4hhb Citations

The crystal structure of human deoxyhaemoglobin at 1.74 A resolution.

J Mol Biol 175 159-74 (1984)
Related entries: 2hhb, 3hhb

Cited: 365 times
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Abstract

The structure of human deoxyhaemoglobin was refined at 1.74 A resolution using data collected on film at room temperature from a synchrotron X-ray source. The crystallographic R-factor is 16.0%. The estimated error in atomic positions is 0.1 A overall, 0.14 A for main-chain atoms of internal segments, and 0.05 A for the iron atoms. The effects of intermolecular contacts on the structure were investigated; such contacts cause only highly localized distortions, as judged from the degree of molecular asymmetry that they induce. The geometry of the iron-nitrogen complex closely resembles that of the deoxymyoglobin structure of Takano (1977) and of the 5-co-ordinated model compounds of Hoard (1975) and Jameson et al. (1980). The distance of the iron from the mean plane of N(porphyrin) is 0.40(5) A and 0.36(5) A, respectively, at the alpha and beta haems, in contrast to the corresponding distance of +0.12(8) A and -0.11(8) A in oxyhaemoglobin ( Shaanan , 1983); the Fe-N epsilon (F8) bond length is 2.12(4) A and the Fe-N(porphyrin) bond length is 2.06(2) A; the last is also in good agreement with extended X-ray fluorescence spectroscopy measurements on deoxyhaemoglobin ( Eisenberger et al., 1978; Perutz et al., 1982). The haems are domed toward the proximal side; the separation between the mean planes of N(porphyrin) and C(porphyrin) being 0.16(6) A and 0.10(6) A, respectively at the alpha and beta haems. At the alpha haems, the normals to the mean pyrrole planes are tilted uniformly toward the haem centre, by about three degrees relative to the haem normal, and there is a folding of about four degrees of the haem about an axis running between the methene carbons that are between the pyrrole rings bearing like-type side-chains. At the beta haems, there is no such folding, and only pyrroles II and IV (those eclipsed by His F8) are appreciably tilted, by about eight degrees. The independence of these parameters from restraints imposed on the model was verified by unrestrained refinement of the entire molecule starting from a structure with modified haem geometry.

Reviews - 4hhb mentioned but not cited (6)

  1. New look at hemoglobin allostery. Yuan Y, Tam MF, Simplaceanu V, Ho C. Chem Rev 115 1702-1724 (2015)
  2. Exploring the computational methods for protein-ligand binding site prediction. Zhao J, Cao Y, Zhang L. Comput Struct Biotechnol J 18 417-426 (2020)
  3. Protein function in precision medicine: deep understanding with machine learning. Rost B, Radivojac P, Bromberg Y. FEBS Lett 590 2327-2341 (2016)
  4. Introduction to molecular replacement: a time perspective. Dodson E. Acta Crystallogr D Struct Biol 77 867-879 (2021)
  5. Dietary Heme-Containing Proteins: Structures, Applications, and Challenges. Xing Y, Gao S, Zhang X, Zang J. Foods 11 3594 (2022)
  6. Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins. Turilli-Ghisolfi ES, Lualdi M, Fasano M. Biomolecules 13 683 (2023)

Articles - 4hhb mentioned but not cited (27)

  1. The RCSB protein data bank: integrative view of protein, gene and 3D structural information. Rose PW, Prlić A, Altunkaya A, Bi C, Bradley AR, Christie CH, Costanzo LD, Duarte JM, Dutta S, Feng Z, Green RK, Goodsell DS, Hudson B, Kalro T, Lowe R, Peisach E, Randle C, Rose AS, Shao C, Tao YP, Valasatava Y, Voigt M, Westbrook JD, Woo J, Yang H, Young JY, Zardecki C, Berman HM, Burley SK. Nucleic Acids Res 45 D271-D281 (2017)
  2. The RCSB Protein Data Bank: redesigned web site and web services. Rose PW, Beran B, Bi C, Bluhm WF, Dimitropoulos D, Goodsell DS, Prlic A, Quesada M, Quinn GB, Westbrook JD, Young J, Yukich B, Zardecki C, Berman HM, Bourne PE. Nucleic Acids Res 39 D392-401 (2011)
  3. SuperPose: a simple server for sophisticated structural superposition. Maiti R, Van Domselaar GH, Zhang H, Wishart DS. Nucleic Acids Res 32 W590-4 (2004)
  4. Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments. Shimizu S. Proc Natl Acad Sci U S A 101 1195-1199 (2004)
  5. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. Viappiani C, Bettati S, Bruno S, Ronda L, Abbruzzetti S, Mozzarelli A, Eaton WA. Proc Natl Acad Sci U S A 101 14414-14419 (2004)
  6. Structure-based predictive models for allosteric hot spots. Demerdash ON, Daily MD, Mitchell JC. PLoS Comput Biol 5 e1000531 (2009)
  7. Real time structural search of the Protein Data Bank. Guzenko D, Burley SK, Duarte JM. PLoS Comput Biol 16 e1007970 (2020)
  8. ProPhylER: a curated online resource for protein function and structure based on evolutionary constraint analyses. Binkley J, Karra K, Kirby A, Hosobuchi M, Stone EA, Sidow A. Genome Res 20 142-154 (2010)
  9. Discovery of the magnetic behavior of hemoglobin: A beginning of bioinorganic chemistry. Bren KL, Eisenberg R, Gray HB. Proc Natl Acad Sci U S A 112 13123-13127 (2015)
  10. In silico analysis of single nucleotide polymorphism (SNPs) in human β-globin gene. Alanazi M, Abduljaleel Z, Khan W, Warsy AS, Elrobh M, Khan Z, Al Amri A, Bazzi MD. PLoS One 6 e25876 (2011)
  11. Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly. Cui W, Zhang H, Blankenship RE, Gross ML. Protein Sci 24 1325-1332 (2015)
  12. Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector. Sahu SC, Simplaceanu V, Gong Q, Ho NT, Tian F, Prestegard JH, Ho C. Biochemistry 46 9973-9980 (2007)
  13. A base measure of precision for protein stability predictors: structural sensitivity. Caldararu O, Blundell TL, Kepp KP. BMC Bioinformatics 22 88 (2021)
  14. Extension of the tryptophan chi2,1 dihedral angle-W3 band frequency relationship to a full rotation: correlations and caveats. Juszczak LJ, Desamero RZ. Biochemistry 48 2777-2787 (2009)
  15. Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex. Winogradoff D, Chou HY, Maffeo C, Aksimentiev A. Nat Commun 13 5138 (2022)
  16. Simplified quality assessment for small-molecule ligands in the Protein Data Bank. Shao C, Westbrook JD, Lu C, Bhikadiya C, Peisach E, Young JY, Duarte JM, Lowe R, Wang S, Rose Y, Feng Z, Burley SK. Structure 30 252-262.e4 (2022)
  17. Blue Light-excited Light-Oxygen-Voltage-sensing Domain 2 (LOV2) Triggers a Rearrangement of the Kinase Domain to Induce Phosphorylation Activity in Arabidopsis Phototropin1. Oide M, Okajima K, Kashojiya S, Takayama Y, Oroguchi T, Hikima T, Yamamoto M, Nakasako M. J Biol Chem 291 19975-19984 (2016)
  18. Arsenic causing gallbladder cancer disease in Bihar. Kumar A, Ali M, Raj V, Kumari A, Rachamalla M, Niyogi S, Kumar D, Sharma A, Saxena A, Panjawani G, Jain P, Vidyarthi A, Kumar N, Kumar M, Niraj PK, Rahman MS, Bishwapriya A, Kumar R, Sakamoto M, Kumar S, Singh M, Ghosh AK. Sci Rep 13 4259 (2023)
  19. Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin. Nacharaju P, Friedman JM, Prabhakaran M, Acharya SA, Manjula BN. Biochemistry 46 4554-4564 (2007)
  20. X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction. Blum MM, Tomanicek SJ, John H, Hanson BL, Rüterjans H, Schoenborn BP, Langan P, Chen JC. Acta Crystallogr Sect F Struct Biol Cryst Commun 66 379-385 (2010)
  21. Fast optimization of statistical potentials for structurally constrained phylogenetic models. Bonnard C, Kleinman CL, Rodrigue N, Lartillot N. BMC Evol Biol 9 227 (2009)
  22. Hemoglobin Einstein: semisynthetic deletion in the B-helix of the alpha-chain. Srinivasulu S, Manjula BN, Nagel RL, Tsai CH, Ho C, Prabhakaran M, Acharya SA. Protein Sci 13 1266-1275 (2004)
  23. Hemoglobin interactions with αB crystallin: a direct test of sensitivity to protein instability. Clark TJ, Houck SA, Clark JI. PLoS One 7 e40486 (2012)
  24. Modulation of hemoglobin dynamics by an allosteric effector. Lal J, Maccarini M, Fouquet P, Ho NT, Ho C, Makowski L. Protein Sci 26 505-514 (2017)
  25. An Improved Strategy for Task Scheduling in the Parallel Computational Alignment of Multiple Sequences. Ishaq M, Khan A, Su'ud MM, Alam MM, Bangash JI, Khan A. Comput Math Methods Med 2022 8691646 (2022)
  26. Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins. Aoto S, Yura K. Biophys Physicobiol 12 103-116 (2015)
  27. Theoretical framework for analyzing structural compliance properties of proteins. Arikawa K. Biophys Physicobiol 15 58-74 (2018)


Reviews citing this publication (29)

  1. The origin of protein interactions and allostery in colocalization. Kuriyan J, Eisenberg D. Nature 450 983-990 (2007)
  2. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Wright HT. Crit Rev Biochem Mol Biol 26 1-52 (1991)
  3. Hydrophobicity: is LogP(o/w) more than the sum of its parts? Eugene Kellogg G, Abraham DJ. Eur J Med Chem 35 651-661 (2000)
  4. The multiple functions of hemoglobin. Giardina B, Messana I, Scatena R, Castagnola M. Crit Rev Biochem Mol Biol 30 165-196 (1995)
  5. Mechanisms of hemoglobin adaptation to high altitude hypoxia. Storz JF, Moriyama H. High Alt Med Biol 9 148-157 (2008)
  6. A tour of structural genomics. Brenner SE. Nat Rev Genet 2 801-809 (2001)
  7. Hemoglobin as a source of endogenous bioactive peptides: the concept of tissue-specific peptide pool. Ivanov VT, Karelin AA, Philippova MM, Nazimov IV, Pletnev VZ. Biopolymers 43 171-188 (1997)
  8. Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications. Liu XR, Zhang MM, Gross ML. Chem Rev 120 4355-4454 (2020)
  9. Transforming growth factor-beta : biology and clinical relevance. Kim IY, Kim MM, Kim SJ. J Biochem Mol Biol 38 1-8 (2005)
  10. Structural divergence and distant relationships in proteins: evolution of the globins. Lecomte JT, Vuletich DA, Lesk AM. Curr Opin Struct Biol 15 290-301 (2005)
  11. Allosteric hemoglobin assembly: diversity and similarity. Royer WE, Zhu H, Gorr TA, Flores JF, Knapp JE. J Biol Chem 280 27477-27480 (2005)
  12. Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers. Turner GJ, Galacteros F, Doyle ML, Hedlund B, Pettigrew DW, Turner BW, Smith FR, Moo-Penn W, Rucknagel DL, Ackers GK. Proteins 14 333-350 (1992)
  13. Molecular aspects of embryonic hemoglobin function. Brittain T. Mol Aspects Med 23 293-342 (2002)
  14. Allosteric modulation of protein oligomerization: an emerging approach to drug design. Gabizon R, Friedler A. Front Chem 2 9 (2014)
  15. How to make big molecules fly out of liquid water: applications, features and physics of laser assisted liquid phase dispersion mass spectrometry. Charvat A, Abel B. Phys Chem Chem Phys 9 3335-3360 (2007)
  16. Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases. Méndez JD, Xie J, Aguilar-Hernández M, Méndez-Valenzuela V. Mol Cell Biochem 344 185-193 (2010)
  17. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Kroeger KS, Kundrot CE. Structure 5 227-237 (1997)
  18. Investigation of higher order structures of proteins by ultraviolet resonance Raman spectroscopy. Kitagawa T. Prog Biophys Mol Biol 58 1-18 (1992)
  19. Miniaturized hemoproteins. Nastri F, Lombardi A, D'Andrea LD, Sanseverino M, Maglio O, Pavone V. Biopolymers 47 5-22 (1998)
  20. Fluorescence line narrowing applied to the study of proteins. Fidy J, Laberge M, Kaposi AD, Vanderkooi JM. Biochim Biophys Acta 1386 331-351 (1998)
  21. Overview of protein structural and functional folds. Sun PD, Foster CE, Boyington JC. Curr Protoc Protein Sci Chapter 17 Unit 17.1 (2004)
  22. A role of heme side-chains of human hemoglobin in its function revealed by circular dichroism and resonance Raman spectroscopy. Nagai M, Mizusawa N, Kitagawa T, Nagatomo S. Biophys Rev 10 271-284 (2018)
  23. Seeing the PDB. Richardson JS, Richardson DC, Goodsell DS. J Biol Chem 296 100742 (2021)
  24. Role of cytoglobin, a novel radical scavenger, in stellate cell activation and hepatic fibrosis. Thuy LTT, Hai H, Kawada N. Clin Mol Hepatol 26 280-293 (2020)
  25. Modulating hemoglobin allostery for treatment of sickle cell disease: current progress and intellectual property. Pagare PP, Rastegar A, Abdulmalik O, Omar AM, Zhang Y, Fleischman A, Safo MK. Expert Opin Ther Pat 32 115-130 (2022)
  26. Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Yang C, Choi M, Kim JG, Kim H, Muniyappan S, Nozawa S, Adachi SI, Henning R, Kosheleva I, Ihee H. Int J Mol Sci 19 E3633 (2018)
  27. Reviving artificial blood: meeting the challenge of dealing with NO scavenging by hemoglobin. Lui FE, Kluger R. Chembiochem 11 1816-1824 (2010)
  28. Allostery: The Rebound of Proteins. Finazzi Agrò A, Mei G. Methods Mol Biol 2253 1-6 (2021)
  29. Transient and time-resolved optical studies of photolyzed carbonmonoxy hemoglobin and myoglobin. Findsen EW, Ondrias MR. Photochem Photobiol 51 741-748 (1990)

Articles citing this publication (303)

  1. Inference of macromolecular assemblies from crystalline state. Krissinel E, Henrick K. J Mol Biol 372 774-797 (2007)
  2. The relation between the divergence of sequence and structure in proteins. Chothia C, Lesk AM. EMBO J 5 823-826 (1986)
  3. Database of homology-derived protein structures and the structural meaning of sequence alignment. Sander C, Schneider R. Proteins 9 56-68 (1991)
  4. Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Katchalski-Katzir E, Shariv I, Eisenstein M, Friesem AA, Aflalo C, Vakser IA. Proc Natl Acad Sci U S A 89 2195-2199 (1992)
  5. Surface, subunit interfaces and interior of oligomeric proteins. Janin J, Miller S, Chothia C. J Mol Biol 204 155-164 (1988)
  6. Improvements in protein secondary structure prediction by an enhanced neural network. Kneller DG, Cohen FE, Langridge R. J Mol Biol 214 171-182 (1990)
  7. Accurate modeling of protein conformation by automatic segment matching. Levitt M. J Mol Biol 226 507-533 (1992)
  8. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. Sali A, Blundell TL. J Mol Biol 212 403-428 (1990)
  9. Topological analysis and interactive visualization of biological networks and protein structures. Doncheva NT, Assenov Y, Domingues FS, Albrecht M. Nat Protoc 7 670-685 (2012)
  10. Suggestions for "safe" residue substitutions in site-directed mutagenesis. Bordo D, Argos P. J Mol Biol 217 721-729 (1991)
  11. Identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean force. Hendlich M, Lackner P, Weitckus S, Floeckner H, Froschauer R, Gottsbacher K, Casari G, Sippl MJ. J Mol Biol 216 167-180 (1990)
  12. A human recombinant haemoglobin designed for use as a blood substitute. Looker D, Abbott-Brown D, Cozart P, Durfee S, Hoffman S, Mathews AJ, Miller-Roehrich J, Shoemaker S, Trimble S, Fermi G. Nature 356 258-260 (1992)
  13. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. Shirakihara Y, Evans PR. J Mol Biol 204 973-994 (1988)
  14. 1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. Park SY, Yokoyama T, Shibayama N, Shiro Y, Tame JR. J Mol Biol 360 690-701 (2006)
  15. Hydrogen bond stereochemistry in protein structure and function. Ippolito JA, Alexander RS, Christianson DW. J Mol Biol 215 457-471 (1990)
  16. Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering. Cammarata M, Levantino M, Schotte F, Anfinrud PA, Ewald F, Choi J, Cupane A, Wulff M, Ihee H. Nat Methods 5 881-886 (2008)
  17. Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations. Sippl MJ, Weitckus S. Proteins 13 258-271 (1992)
  18. Target flexibility: an emerging consideration in drug discovery and design. Cozzini P, Kellogg GE, Spyrakis F, Abraham DJ, Costantino G, Emerson A, Fanelli F, Gohlke H, Kuhn LA, Morris GM, Orozco M, Pertinhez TA, Rizzi M, Sotriffer CA. J Med Chem 51 6237-6255 (2008)
  19. Hydrophobic docking: a proposed enhancement to molecular recognition techniques. Vakser IA, Aflalo C. Proteins 20 320-329 (1994)
  20. Volume changes in protein evolution. Gerstein M, Sonnhammer EL, Chothia C. J Mol Biol 236 1067-1078 (1994)
  21. Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients. Abraham DJ, Leo AJ. Proteins 2 130-152 (1987)
  22. The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: implications for the design of hemoglobin-based oxygen carriers. McCarthy MR, Vandegriff KD, Winslow RM. Biophys Chem 92 103-117 (2001)
  23. Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering. Jessen TH, Weber RE, Fermi G, Tame J, Braunitzer G. Proc Natl Acad Sci U S A 88 6519-6522 (1991)
  24. Crystal structure of a nonsymbiotic plant hemoglobin. Hargrove MS, Brucker EA, Stec B, Sarath G, Arredondo-Peter R, Klucas RV, Olson JS, Phillips GN. Structure 8 1005-1014 (2000)
  25. Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution. Ermler U, Siddiqui RA, Cramm R, Friedrich B. EMBO J 14 6067-6077 (1995)
  26. Detection of common three-dimensional substructures in proteins. Vriend G, Sander C. Proteins 11 52-58 (1991)
  27. Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. Nagai K, Perutz MF, Poyart C. Proc Natl Acad Sci U S A 82 7252-7255 (1985)
  28. The high resolution crystal structure of deoxyhemoglobin S. Harrington DJ, Adachi K, Royer WE. J Mol Biol 272 398-407 (1997)
  29. Electrostatics in protein-protein docking. Heifetz A, Katchalski-Katzir E, Eisenstein M. Protein Sci 11 571-587 (2002)
  30. Taxonomy and conformational analysis of loops in proteins. Ring CS, Kneller DG, Langridge R, Cohen FE. J Mol Biol 224 685-699 (1992)
  31. Low-resolution docking: prediction of complexes for underdetermined structures. Vakser IA. Biopolymers 39 455-464 (1996)
  32. Novel method for the rapid evaluation of packing in protein structures. Gregoret LM, Cohen FE. J Mol Biol 211 959-974 (1990)
  33. Broad-spectrum antimicrobial activity of hemoglobin. Parish CA, Jiang H, Tokiwa Y, Berova N, Nakanishi K, McCabe D, Zuckerman W, Xia MM, Gabay JE. Bioorg Med Chem 9 377-382 (2001)
  34. Non-functional conserved residues in globins and their possible role as a folding nucleus. Ptitsyn OB, Ting KL. J Mol Biol 291 671-682 (1999)
  35. Porphyrins as theranostic agents from prehistoric to modern times. Zhang Y, Lovell JF. Theranostics 2 905-915 (2012)
  36. General architecture of the alpha-helical globule. Murzin AG, Finkelstein AV. J Mol Biol 204 749-769 (1988)
  37. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nagai K, Luisi B, Shih D, Miyazaki G, Imai K, Poyart C, De Young A, Kwiatkowsky L, Noble RW, Lin SH. Nature 329 858-860 (1987)
  38. Distribution and complementarity of hydropathy in multisubunit proteins. Korn AP, Burnett RM. Proteins 9 37-55 (1991)
  39. A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead in sequence: their occurrence at alpha-helical N termini and in other situations. Wan WY, Milner-White EJ. J Mol Biol 286 1633-1649 (1999)
  40. Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering. Kim KH, Muniyappan S, Oang KY, Kim JG, Nozawa S, Sato T, Koshihara SY, Henning R, Kosheleva I, Ki H, Kim Y, Kim TW, Kim J, Adachi S, Ihee H. J Am Chem Soc 134 7001-7008 (2012)
  41. High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin. Liddington R, Derewenda Z, Dodson E, Hubbard R, Dodson G. J Mol Biol 228 551-579 (1992)
  42. Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases. Larsen R, Gouveia Z, Soares MP, Gozzelino R. Front Pharmacol 3 77 (2012)
  43. Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin. Knapp JE, Pahl R, Srajer V, Royer WE. Proc Natl Acad Sci U S A 103 7649-7654 (2006)
  44. Electrostatic properties of protein-protein complexes. Kundrotas PJ, Alexov E. Biophys J 91 1724-1736 (2006)
  45. Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics. Laberge M, Yonetani T. Biophys J 94 2737-2751 (2008)
  46. Lecture The emergence of protein complexes: quaternary structure, dynamics and allostery. Colworth Medal Lecture. Perica T, Marsh JA, Sousa FL, Natan E, Colwell LJ, Ahnert SE, Teichmann SA. Biochem Soc Trans 40 475-491 (2012)
  47. Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins. Johnson MS, Sutcliffe MJ, Blundell TL. J Mol Evol 30 43-59 (1990)
  48. Comparison of the structures of globins and phycocyanins: evidence for evolutionary relationship. Pastore A, Lesk AM. Proteins 8 133-155 (1990)
  49. Protein structure alignment using a genetic algorithm. Szustakowski JD, Weng Z. Proteins 38 428-440 (2000)
  50. Deoxymyoglobin studied by the conformational normal mode analysis. I. Dynamics of globin and the heme-globin interaction. Seno Y, Go N. J Mol Biol 216 95-109 (1990)
  51. Unsuspected pathway of the allosteric transition in hemoglobin. Fischer S, Olsen KW, Nam K, Karplus M. Proc Natl Acad Sci U S A 108 5608-5613 (2011)
  52. Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. Camardella L, Caruso C, D'Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF. J Mol Biol 224 449-460 (1992)
  53. Optical absorption spectra of deoxy- and oxyhemoglobin in the temperature range 300-20 K. Relation with protein dynamics. Cordone L, Cupane A, Leone M, Vitrano E. Biophys Chem 24 259-275 (1986)
  54. Raman microspectroscopy and imaging provides insights into heme aggregation and denaturation within human erythrocytes. Wood BR, Hammer L, Davis L, McNaughton D. J Biomed Opt 10 14005 (2005)
  55. The T-to-R transformation in hemoglobin: a reevaluation. Srinivasan R, Rose GD. Proc Natl Acad Sci U S A 91 11113-11117 (1994)
  56. The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG. Proteins 10 50-69 (1991)
  57. The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase. Wierenga RK, Noble ME, Postma JP, Groendijk H, Kalk KH, Hol WG, Opperdoes FR. Proteins 10 33-49 (1991)
  58. Allosteric transition intermediates modelled by crosslinked haemoglobins. Schumacher MA, Dixon MM, Kluger R, Jones RT, Brennan RG. Nature 375 84-87 (1995)
  59. The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin. Smith FR, Lattman EE, Carter CW. Proteins 10 81-91 (1991)
  60. Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation. Seno Y, Go N. J Mol Biol 216 111-126 (1990)
  61. New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations. Mouawad L, Perahia D, Robert CH, Guilbert C. Biophys J 82 3224-3245 (2002)
  62. The crystal structure of a tetrameric hemoglobin in a partial hemichrome state. Riccio A, Vitagliano L, di Prisco G, Zagari A, Mazzarella L. Proc Natl Acad Sci U S A 99 9801-9806 (2002)
  63. Crystal structure of unliganded phosphofructokinase from Escherichia coli. Rypniewski WR, Evans PR. J Mol Biol 207 805-821 (1989)
  64. Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin. Smith FR, Ackers GK. Proc Natl Acad Sci U S A 82 5347-5351 (1985)
  65. Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding. Liddington R, Derewenda Z, Dodson G, Harris D. Nature 331 725-728 (1988)
  66. Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Simplaceanu V, Lukin JA, Fang TY, Zou M, Ho NT, Ho C. Biophys J 79 1146-1154 (2000)
  67. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. Lukin JA, Simplaceanu V, Zou M, Ho NT, Ho C. Proc Natl Acad Sci U S A 97 10354-10358 (2000)
  68. Quantification of tertiary structural conservation despite primary sequence drift in the globin fold. Aronson HE, Royer WE, Hendrickson WA. Protein Sci 3 1706-1711 (1994)
  69. Spontaneous quaternary and tertiary T-R transitions of human hemoglobin in molecular dynamics simulation. Hub JS, Kubitzki MB, de Groot BL. PLoS Comput Biol 6 e1000774 (2010)
  70. Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Bell JA, Wilson KP, Zhang XJ, Faber HR, Nicholson H, Matthews BW. Proteins 10 10-21 (1991)
  71. Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. Henry ER, Levitt M, Eaton WA. Proc Natl Acad Sci U S A 82 2034-2038 (1985)
  72. Rigid domains in proteins: an algorithmic approach to their identification. Nichols WL, Rose GD, Ten Eyck LF, Zimm BH. Proteins 23 38-48 (1995)
  73. The RCSB PDB "Molecule of the Month": Inspiring a Molecular View of Biology. Goodsell DS, Dutta S, Zardecki C, Voigt M, Berman HM, Burley SK. PLoS Biol 13 e1002140 (2015)
  74. Evolution of protein cores. Constraints in point mutations as observed in globin tertiary structures. Bordo D, Argos P. J Mol Biol 211 975-988 (1990)
  75. Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity. Lacan P, Kister J, Francina A, Souillet G, Galactéros F, Delaunay J, Wajcman H. Am J Hematol 51 276-281 (1996)
  76. Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study. Gronenborn AM, Clore GM, Brunori M, Giardina B, Falcioni G, Perutz MF. J Mol Biol 178 731-742 (1984)
  77. Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building. Adzhubei AA, Sternberg MJ. Protein Sci 3 2395-2410 (1994)
  78. Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. Nicholson H, Söderlind E, Tronrud DE, Matthews BW. J Mol Biol 210 181-193 (1989)
  79. Detecting single atoms of calcium and iron in biological structures by electron energy-loss spectrum-imaging. Leapman RD. J Microsc 210 5-15 (2003)
  80. Direct observation of photolysis-induced tertiary structural changes in hemoglobin. Adachi S, Park SY, Tame JR, Shiro Y, Shibayama N. Proc Natl Acad Sci U S A 100 7039-7044 (2003)
  81. Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state. Svergun DI, Barberato C, Koch MH, Fetler L, Vachette P. Proteins 27 110-117 (1997)
  82. Hydropathic analysis of the non-covalent interactions between molecular subunits of structurally characterized hemoglobins. Abraham DJ, Kellogg GE, Holt JM, Ackers GK. J Mol Biol 272 613-632 (1997)
  83. Micro-Raman characterization of high- and low-spin heme moieties within single living erythrocytes. Wood BR, McNaughton D. Biopolymers 67 259-262 (2002)
  84. The structural and functional analysis of the hemoglobin D component from chicken. Knapp JE, Oliveira MA, Xie Q, Ernst SR, Riggs AF, Hackert ML. J Biol Chem 274 6411-6420 (1999)
  85. Very empirical treatment of solvation and entropy: a force field derived from log Po/w. Kellogg GE, Burnett JC, Abraham DJ. J Comput Aided Mol Des 15 381-393 (2001)
  86. COVOL: an interactive program for evaluating second virial coefficients from the triaxial shape or dimensions of rigid macromolecules. Harding SE, Horton JC, Jones S, Thornton JM, Winzor DJ. Biophys J 76 2432-2438 (1999)
  87. A procedure for the automatic determination of hydrophobic cores in protein structures. Swindells MB. Protein Sci 4 93-102 (1995)
  88. Computationally accessible method for estimating free energy changes resulting from site-specific mutations of biomolecules: systematic model building and structural/hydropathic analysis of deoxy and oxy hemoglobins. Burnett JC, Botti P, Abraham DJ, Kellogg GE. Proteins 42 355-377 (2001)
  89. Pseudo 2-fold symmetry in the copper-binding domain of arthropodan haemocyanins. Possible implications for the evolution of oxygen transport proteins. Volbeda A, Hol WG. J Mol Biol 206 531-546 (1989)
  90. Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli. Weickert MJ, Pagratis M, Curry SR, Blackmore R. Appl Environ Microbiol 63 4313-4320 (1997)
  91. High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector. Safo MK, Moure CM, Burnett JC, Joshi GS, Abraham DJ. Protein Sci 10 951-957 (2001)
  92. Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation. Samuni U, Roche CJ, Dantsker D, Juszczak LJ, Friedman JM. Biochemistry 45 2820-2835 (2006)
  93. NMR investigation of the dynamics of tryptophan side-chains in hemoglobins. Yuan Y, Simplaceanu V, Lukin JA, Ho C. J Mol Biol 321 863-878 (2002)
  94. Structural and evolutionary versatility in protein complexes with uneven stoichiometry. Marsh JA, Rees HA, Ahnert SE, Teichmann SA. Nat Commun 6 6394 (2015)
  95. Structure of deoxy-quaternary haemoglobin with liganded beta subunits. Luisi B, Liddington B, Fermi G, Shibayama N. J Mol Biol 214 7-14 (1990)
  96. Restoring allosterism with compensatory mutations in hemoglobin. Kim HW, Shen TJ, Sun DP, Ho NT, Madrid M, Tam MF, Zou M, Cottam PF, Ho C. Proc Natl Acad Sci U S A 91 11547-11551 (1994)
  97. The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1 A resoultion and its relationship to the quaternary structures of other hemoglobin crystal froms. Safo MK, Abraham DJ. Protein Sci 10 1091-1099 (2001)
  98. Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure. Smith FR, Simmons KC. Proteins 18 295-300 (1994)
  99. Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study. Jones EM, Monza E, Balakrishnan G, Blouin GC, Mak PJ, Zhu Q, Kincaid JR, Guallar V, Spiro TG. J Am Chem Soc 136 10325-10339 (2014)
  100. Haemoglobin: the surface buried between the alpha 1 beta 1 and alpha 2 beta 2 dimers in the deoxy and oxy structures. Lesk AM, Janin J, Wodak S, Chothia C. J Mol Biol 183 267-270 (1985)
  101. Significance of structural changes in proteins: expected errors in refined protein structures. Stroud RM, Fauman EB. Protein Sci 4 2392-2404 (1995)
  102. A comparative NMR study of the polypeptide backbone dynamics of hemoglobin in the deoxy and carbonmonoxy forms. Song XJ, Yuan Y, Simplaceanu V, Sahu SC, Ho NT, Ho C. Biochemistry 46 6795-6803 (2007)
  103. Allosteric intermediates indicate R2 is the liganded hemoglobin end state. Schumacher MA, Zheleznova EE, Poundstone KS, Kluger R, Jones RT, Brennan RG. Proc Natl Acad Sci U S A 94 7841-7844 (1997)
  104. Electrostatics of hemoglobins from measurements of the electric dichroism and computer simulations. Antosiewicz J, Porschke D. Biophys J 68 655-664 (1995)
  105. Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling. Balakrishnan G, Tsai CH, Wu Q, Case MA, Pevsner A, McLendon GL, Ho C, Spiro TG. J Mol Biol 340 857-868 (2004)
  106. Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme. Miyazaki G, Morimoto H, Yun KM, Park SY, Nakagawa A, Minagawa H, Shibayama N. J Mol Biol 292 1121-1136 (1999)
  107. The quaternary structure of carbonmonoxy hemoglobin ypsilanti. Janin J, Wodak SJ. Proteins 15 1-4 (1993)
  108. What is the true structure of liganded haemoglobin? Tame JR. Trends Biochem Sci 24 372-377 (1999)
  109. Acetylcholine receptor-alpha-bungarotoxin interactions: determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Ruan KH, Spurlino J, Quiocho FA, Atassi MZ. Proc Natl Acad Sci U S A 87 6156-6160 (1990)
  110. Functional role of the distal valine (E11) residue of alpha subunits in human haemoglobin. Tame J, Shih DT, Pagnier J, Fermi G, Nagai K. J Mol Biol 218 761-767 (1991)
  111. O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: structural and functional consequences of beta93Cys modification. Boykins RA, Buehler PW, Jia Y, Venable R, Alayash AI. Proteins 59 840-855 (2005)
  112. Sequence alignment approach to pick up conformationally similar protein fragments. Kolaskar AS, Kulkarni-Kale U. J Mol Biol 223 1053-1061 (1992)
  113. Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems. Luisi B, Shibayama N. J Mol Biol 206 723-736 (1989)
  114. The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap between macromolecular and small molecule crystallography. Kang BS, Devedjiev Y, Derewenda U, Derewenda ZS. J Mol Biol 338 483-493 (2004)
  115. Doming modes and dynamics of model heme compounds. Klug DD, Zgierski MZ, Tse JS, Liu Z, Kincaid JR, Czarnecki K, Hemley RJ. Proc Natl Acad Sci U S A 99 12526-12530 (2002)
  116. Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds. Kneipp J, Balakrishnan G, Chen R, Shen TJ, Sahu SC, Ho NT, Giovannelli JL, Simplaceanu V, Ho C, Spiro TG. J Mol Biol 356 335-353 (2006)
  117. Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study. Jones EM, Balakrishnan G, Spiro TG. J Am Chem Soc 134 3461-3471 (2012)
  118. Multiscale Molecular Dynamics Simulation of Multiple Protein Adsorption on Gold Nanoparticles. Tavanti F, Pedone A, Menziani MC. Int J Mol Sci 20 E3539 (2019)
  119. Structural and functional analysis of the two haemoglobins of the antarctic seabird Catharacta maccormicki characterization of an additional phosphate binding site by molecular modelling. Tamburrini M, Riccio A, Romano M, Giardina B, di Prisco G. Eur J Biochem 267 6089-6098 (2000)
  120. Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode. Gilch H, Schweitzer-Stenner R, Dreybrodt W. Biophys J 65 1470-1485 (1993)
  121. Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan beta 37 mutant. Nagai M, Kaminaka S, Ohba Y, Nagai Y, Mizutani Y, Kitagawa T. J Biol Chem 270 1636-1642 (1995)
  122. X-ray diffraction studies of a partially liganded hemoglobin, [alpha(FeII-CO)beta(MnII)]2. Arnone A, Rogers P, Blough NV, McGourty JL, Hoffman BM. J Mol Biol 188 693-706 (1986)
  123. X-ray diffraction study of di and tetra-ligated T-state hemoglobin from high salt crystals. Abraham DJ, Peascoe RA, Randad RS, Panikker J. J Mol Biol 227 480-492 (1992)
  124. Aspergillus niger Prolyl Endoprotease for Hydrogen-Deuterium Exchange Mass Spectrometry and Protein Structural Studies. Tsiatsiani L, Akeroyd M, Olsthoorn M, Heck AJR. Anal Chem 89 7966-7973 (2017)
  125. Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin. Song XJ, Simplaceanu V, Ho NT, Ho C. Biochemistry 47 4907-4915 (2008)
  126. Low-dose cryo electron ptychography via non-convex Bayesian optimization. Pelz PM, Qiu WX, Bücker R, Kassier G, Miller RJD. Sci Rep 7 9883 (2017)
  127. Photoselection in polarized photolysis experiments on heme proteins. Ansari A, Jones CM, Henry ER, Hofrichter J, Eaton WA. Biophys J 64 852-868 (1993)
  128. Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry. Zhu Y, Cheng G, Dong S. Biophys Chem 97 129-138 (2002)
  129. Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange. Louie G, Tran T, Englander JJ, Englander SW. J Mol Biol 201 755-764 (1988)
  130. Coarse-grained and all-atom modeling of structural states and transitions in hemoglobin. Tekpinar M, Zheng W. Proteins 81 240-252 (2013)
  131. Combining hydrophobicity and helicity: a novel approach to membrane protein structure prediction. Liu LP, Deber CM. Bioorg Med Chem 7 1-7 (1999)
  132. Intrinsic energy landscapes of amino acid side-chains. Zhu X, Lopes PE, Shim J, MacKerell AD. J Chem Inf Model 52 1559-1572 (2012)
  133. R-state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites. Laberge M, Kövesi I, Yonetani T, Fidy J. FEBS Lett 579 627-632 (2005)
  134. The fold of human aquaporin 1. de Groot BL, Heymann JB, Engel A, Mitsuoka K, Fujiyoshi Y, Grubmüller H. J Mol Biol 300 987-994 (2000)
  135. A new mode for heme-heme interactions in hemoglobin associated with distal perturbations. Levy A, Sharma VS, Zhang L, Rifkind JM. Biophys J 61 750-755 (1992)
  136. Collective dynamics underlying allosteric transitions in hemoglobin. Vesper MD, de Groot BL. PLoS Comput Biol 9 e1003232 (2013)
  137. Comparing short protein substructures by a method based on backbone torsion angles. Karpen ME, de Haseth PL, Neet KE. Proteins 6 155-167 (1989)
  138. Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function. Thompson MK, Davis MF, de Serrano V, Nicoletti FP, Howes BD, Smulevich G, Franzen S. Biophys J 99 1586-1595 (2010)
  139. The effect of water on the rate of conformational change in protein allostery. Goldbeck RA, Paquette SJ, Kliger DS. Biophys J 81 2919-2934 (2001)
  140. Thermal stability of hemoglobin crosslinked in the T-state by bis(3,5-dibromosalicyl) fumarate. Yang T, Olsen KW. Biochem Biophys Res Commun 174 518-523 (1991)
  141. A fast unbiased comparison of protein structures by means of the Needleman-Wunsch algorithm. Rose J, Eisenmenger F. J Mol Evol 32 340-354 (1991)
  142. Comparison of protein surfaces using a genetic algorithm. Poirrette AR, Artymiuk PJ, Rice DW, Willett P. J Comput Aided Mol Des 11 557-569 (1997)
  143. Crystallographic analysis of mutant human haemoglobins made in Escherichia coli. Luisi BF, Nagai K. Nature 320 555-556 (1986)
  144. Probing the biological evaluations of a new designed Pt(II) complex using spectroscopic and theoretical approaches: human hemoglobin as a target. Abazari O, Shafaei Z, Divsalar A, Eslami-Moghadam M, Ghalandari B, Saboury AA. J Biomol Struct Dyn 34 1123-1131 (2016)
  145. Quantitative symmetry and chirality--a fast computational algorithm for large structures: proteins, macromolecules, nanotubes, and unit cells. Dryzun C, Zait A, Avnir D. J Comput Chem 32 2526-2538 (2011)
  146. Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin. Perutz MF, Fermi G, Shih TB. Proc Natl Acad Sci U S A 81 4781-4784 (1984)
  147. The functional similarity and structural diversity of human and cartilaginous fish hemoglobins. Naoi Y, Chong KT, Yoshimatsu K, Miyazaki G, Tame JR, Park SY, Adachi S, Morimoto H. J Mol Biol 307 259-270 (2001)
  148. Charge-gated transport of proteins in nanostructured optical films of mesoporous silica. Chen MY, Sailor MJ. Anal Chem 83 7186-7193 (2011)
  149. Conservation of metal-coordinating residues. Kasampalidis IN, Pitas I, Lyroudia K. Proteins 68 123-130 (2007)
  150. Letter Dynamics of haemoglobin. Kagan VE, Day BW, Elsayed NM, Gorbunov NV. Nature 383 30-31 (1996)
  151. Effects of NaCl on the linkages between O2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. Doyle ML, Holt JM, Ackers GK. Biophys Chem 64 271-287 (1997)
  152. Kinetic spectroscopy of heme hydration and ligand binding in myoglobin and isolated hemoglobin chains: an optical window into heme pocket water dynamics. Esquerra RM, López-Peña I, Tipgunlakant P, Birukou I, Nguyen RL, Soman J, Olson JS, Kliger DS, Goldbeck RA. Phys Chem Chem Phys 12 10270-10278 (2010)
  153. Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south polar skua. Is there a site-site migratory mechanism along the central cavity? Riccio A, Tamburrini M, Giardina B, di Prisco G. Biophys J 81 1938-1946 (2001)
  154. Acid Bohr effect of a monomeric haemoglobin from Dicrocoelium dendriticum. Mechanism of the allosteric conformation transition. Smit JD, Sick H, Peterhans A, Gersonde K. Eur J Biochem 155 231-237 (1986)
  155. Conformation-invariant structures of the alpha1beta1 human hemoglobin dimer. Nichols WL, Zimm BH, Ten Eyck LF. J Mol Biol 270 598-615 (1997)
  156. Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering. Kim JG, Muniyappan S, Oang KY, Kim TW, Yang C, Kim KH, Kim J, Ihee H. Struct Dyn 3 023610 (2016)
  157. Hydrophobic interaction between globin helices. Weaver DL. Biopolymers 32 477-490 (1992)
  158. N-terminal contributions of the gamma-subunit of fetal hemoglobin to its tetramer strength: remote effects at subunit contacts. Yagami T, Ballard BT, Padovan JC, Chait BT, Popowicz AM, Manning JM. Protein Sci 11 27-35 (2002)
  159. Signal transmission between subunits in the hemoglobin T-state. Englander JJ, Rumbley JN, Englander SW. J Mol Biol 284 1707-1716 (1998)
  160. The pH dependence of heme pocket hydration and ligand rebinding kinetics in photodissociated carbonmonoxymyoglobin. Esquerra RM, Jensen RA, Bhaskaran S, Pillsbury ML, Mendoza JL, Lintner BW, Kliger DS, Goldbeck RA. J Biol Chem 283 14165-14175 (2008)
  161. X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin. Wireko FC, Abraham DJ. Proc Natl Acad Sci U S A 88 2209-2211 (1991)
  162. Apparent specific volume of human hemoglobin: effect of ligand state and contribution of heme. DeMoll E, Cox DJ, Daniel E, Riggs AF. Anal Biochem 363 196-203 (2007)
  163. Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination. Nothnagel HJ, Preimesberger MR, Pond MP, Winer BY, Adney EM, Lecomte JT. J Biol Inorg Chem 16 539-552 (2011)
  164. Destructive effect of anticancer oxali-palladium on heme degradation through the generation of endogenous hydrogen peroxide. Abbasi-Tajarag K, Divsalar A, Saboury AA, Ghalandari B, Ghourchian H. J Biomol Struct Dyn 34 2493-2504 (2016)
  165. Effect of T-R conformational change on sickle-cell hemoglobin interactions and aggregation. Vaiana SM, Rotter MA, Emanuele A, Ferrone FA, Palma-Vittorelli MB. Proteins 58 426-438 (2005)
  166. Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia. Kidd RD, Baker HM, Mathews AJ, Brittain T, Baker EN. Protein Sci 10 1739-1749 (2001)
  167. Potential Modulation of Vascular Function by Nitric Oxide and Reactive Oxygen Species Released From Erythrocytes. Rifkind JM, Mohanty JG, Nagababu E, Salgado MT, Cao Z. Front Physiol 9 690 (2018)
  168. Structure, function and molecular adaptations of haemoglobins of the polar cartilaginous fish Bathyraja eatonii and Raja hyperborea. Verde C, De Rosa MC, Giordano D, Mosca D, De Pascale D, Raiola L, Cocca E, Carratore V, Giardina B, Di Prisco G. Biochem J 389 297-306 (2005)
  169. The near-symmetry of proteins. Bonjack-Shterengartz M, Avnir D. Proteins 83 722-734 (2015)
  170. An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate. Yuan Y, Simplaceanu V, Ho NT, Ho C. Biochemistry 49 10606-10615 (2010)
  171. Contribution of alpha140Tyr and beta37Trp to the near-UV CD spectra on quaternary structure transition of human hemoglobin A. Li R, Nagai Y, Nagai M. Chirality 12 216-220 (2000)
  172. Local Fe site structure in the tense-to-relaxed transition in carp deoxyhemoglobin: a XANES (x-ray absorption near edge structure) study. Bianconi A, Congiu-Castellano A, Dell'Ariccia M, Giovannelli A, Morante S, Burattini E, Durham PJ. Proc Natl Acad Sci U S A 83 7736-7740 (1986)
  173. Low frequency resonance Raman spectra of isolated alpha and beta subunits of hemoglobin and their deuterated analogues. Podstawka E, Mak PJ, Kincaid JR, Proniewicz LM. Biopolymers 83 455-466 (2006)
  174. Organotin-protein interactions. Binding of triethyltin bromide to cat haemoglobin. Siebenlist KR, Taketa F. Biochem J 233 471-477 (1986)
  175. Rates of energy transfer between tryptophans and hemes in hemoglobin, assuming that the heme is a planar oscillator. Gryczynski Z, Tenenholz T, Bucci E. Biophys J 63 648-653 (1992)
  176. Amino-acid sequences and functional differentiation of hemoglobins A and D from swift (Apus apus, Apodiformes). Nothum R, Weber RE, Kösters J, Schneeganss D, Braunitzer G. Biol Chem Hoppe Seyler 370 1197-1207 (1989)
  177. Effect of the abolition of intersubunit salt bridges on allosteric protein structural dynamics. Choi M, Kim JG, Muniyappan S, Kim H, Kim TW, Lee Y, Lee SJ, Kim SO, Ihee H. Chem Sci 12 8207-8217 (2021)
  178. Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers. Baudin V, Pagnier J, Kiger L, Kister J, Schaad O, Bihoreau MT, Lacaze N, Marden MC, Edelstein SJ, Poyart C. Protein Sci 2 1320-1330 (1993)
  179. Residue-residue contact substitution probabilities derived from aligned three-dimensional structures and the identification of common folds. Rodionov MA, Johnson MS. Protein Sci 3 2366-2377 (1994)
  180. Role of water molecules in the crystal structure of Gly-L-Ala-L-Phe: a possible sequence preference for nucleation of alpha-helix? Ramasubbu N, Parthasarathy R. Biopolymers 28 1259-1269 (1989)
  181. A quantitative methodology for the de novo design of proteins. Brenner SE, Berry A. Protein Sci 3 1871-1882 (1994)
  182. Dimer-tetramer association equilibria of human adult hemoglobin and its mutants as observed by analytical ultracentrifugation. Arisaka F, Nagai Y, Nagai M. Methods 54 175-180 (2011)
  183. Hb Arta [beta 45 (CD4) Phe-->Cys]: a new unstable haemoglobin with reduced oxygen affinity in trans with beta-thalassaemia. Vassilopoulos G, Papassotiriou I, Voskaridou E, Stamoulakatou A, Premetis E, Kister J, Marden M, Griffon N, Poyart C, Wajcman H. Br J Haematol 91 595-601 (1995)
  184. Hemoglobin Chico [beta 66(E10)Lys----Thr]: a new variant with decreased oxygen affinity. Shih DT, Jones RT, Shih MF, Jones MB, Koler RD, Howard J. Hemoglobin 11 453-464 (1987)
  185. Hemoglobin allostery: new views on old players. Miele AE, Bellelli A, Brunori M. J Mol Biol 425 1515-1526 (2013)
  186. High frequency dynamics in hemoglobin measured by magnetic relaxation dispersion. Victor K, Van-Quynh A, Bryant RG. Biophys J 88 443-454 (2005)
  187. Improving Luminol Blood Detection in Forensics. Stoica BA, Bunescu S, Neamtu A, Bulgaru-Iliescu D, Foia L, Botnariu EG. J Forensic Sci 61 1331-1336 (2016)
  188. Phthalide Derivatives from Angelica Sinensis Decrease Hemoglobin Oxygen Affinity: A New Allosteric-Modulating Mechanism and Potential Use as 2,3-BPG Functional Substitutes. Chen WR, Yu Y, Zulfajri M, Lin PC, Wang CC. Sci Rep 7 5504 (2017)
  189. Protein conformational dynamics of homodimeric hemoglobin revealed by combined time-resolved spectroscopic probes. Choi J, Muniyappan S, Wallis JT, Royer WE, Ihee H. Chemphyschem 11 109-114 (2010)
  190. Spectroscopic properties of the nitric oxide derivative of ferrous man, horse, and ruminant hemoglobins: a comparative study. Ascenzi P, Coletta M, Desideri A, Petruzzelli R, Polizio F, Bolognesi M, Condò SG, Giardina B. J Inorg Biochem 45 31-37 (1992)
  191. The side-by-side model of two tRNA molecules allowing the alpha-helical conformation of the nascent polypeptide during the ribosomal transpeptidation. Nagano K, Takagi H, Harel M. Biochimie 73 947-960 (1991)
  192. A 45-ns molecular dynamics simulation of hemoglobin in water by vectorizing and parallelizing COSMOS90 on the earth simulator: dynamics of tertiary and quaternary structures. Saito M, Okazaki I. J Comput Chem 28 1129-1136 (2007)
  193. A DFT study on the relative affinity for oxygen of the alpha and beta subunits of hemoglobin. Maréchal JD, Maseras F, Lledós A, Mouawad L, Perahia D. J Comput Chem 27 1446-1453 (2006)
  194. Autoxidation and oxygen binding properties of recombinant hemoglobins with substitutions at the αVal-62 or βVal-67 position of the distal heme pocket. Tam MF, Rice NW, Maillett DH, Simplaceanu V, Ho NT, Tam TCS, Shen TJ, Ho C. J Biol Chem 288 25512-25521 (2013)
  195. Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate. Fernandez EJ, Abad-Zapatero C, Olsen KW. J Mol Biol 296 1245-1256 (2000)
  196. Dominant beta-thalassaemia: a highly unstable haemoglobin is caused by a novel 6 bp deletion of the beta-globin gene. Vetter B, Neu-Yilik G, Kohne E, Arnold R, Sinha P, Gaedicke G, Ivancevic V, Kulozik AE. Br J Haematol 108 176-181 (2000)
  197. Features of S-nitrosylation based on statistical analysis and molecular dynamics simulation: cysteine acidity, surrounding basicity, steric hindrance and local flexibility. Cheng S, Shi T, Wang XL, Liang J, Wu H, Xie L, Li Y, Zhao YL. Mol Biosyst 10 2597-2606 (2014)
  198. Molecular modeling studies of surface decoration of hemoglobin by maleimide PEG. Prabhakaran M, Manjula BN, Acharya SA. Artif Cells Blood Substit Immobil Biotechnol 34 381-393 (2006)
  199. Probing the conformation of hemoglobin presbyterian in the R-state. Acharya SA, Malavalli A, Peterson E, Sun PD, Ho C, Prabhakaran M, Arnone A, Manjula BN, Friedman JM. J Protein Chem 22 221-230 (2003)
  200. Structures and oxygen affinities of crystalline human hemoglobin C (β6 Glu->Lys) in the R and R2 quaternary structures. Shibayama N, Sugiyama K, Park SY. J Biol Chem 286 33661-33668 (2011)
  201. Thermal stability and cross-linking of Hb New York [beta 113(G15)Val----Glu]. Yang T, Olsen KW. Hemoglobin 13 147-156 (1989)
  202. Acetaminophen interacts with human hemoglobin: optical, physical and molecular modeling studies. Seal P, Sikdar J, Roy A, Haldar R. J Biomol Struct Dyn 35 1307-1321 (2017)
  203. Allosteric free energy changes at the alpha 1 beta 2 interface of human hemoglobin probed by proton exchange of Trp beta 37. Mihailescu MR, Fronticelli C, Russu IM. Proteins 44 73-78 (2001)
  204. Binding of hydroxylated single-walled carbon nanotubes to two hemoproteins, hemoglobin and myoglobin. Wang YQ, Zhang HM, Cao J. J Photochem Photobiol B 141 26-35 (2014)
  205. Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution. Shirai T, Fujikake M, Yamane T, Inaba K, Ishimori K, Morishima I. J Mol Biol 287 369-382 (1999)
  206. Determination of ligand conformation in macromolecular complexes using the transferred nuclear Overhauser effect. Gronenborn AM, Clore GM. Biochem Pharmacol 40 115-119 (1990)
  207. HbS-Savaria: the anti-polymerization effect of a single mutation in human alpha-chains. Srinivasulu S, Acharya AS, Prabhakaran M, Fabry ME, Alami R, Fiering SN, Bouhasirra EE, Nagel RL. Protein J 26 523-532 (2007)
  208. Introduction of a new regulatory mechanism into human hemoglobin. Fronticelli C, Bobofchak KM, Karavitis M, Sanna MT, Brinigar WS. Biophys Chem 98 115-126 (2002)
  209. Linear dichroism study of metalloporphyrin transition moments in view of radiationless interactions with tryptophan in hemoproteins. Gryczynski Z, Bucci E, Kuśba J. Photochem Photobiol 58 492-498 (1993)
  210. Molecular illustration in black and white. Goodsell DS, Olson AJ. J Mol Graph 10 235-240 (1992)
  211. Secondary structure prediction for the spectrin 106-amino acid segment, and a proposed model for tertiary structure. Xu Y, Prabhakaran M, Johnson ME, Fung LW. J Biomol Struct Dyn 8 55-62 (1990)
  212. Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation. Tsai CH, Simplaceanu V, Ho NT, Shen TJ, Wang D, Spiro TG, Ho C. Biophys Chem 100 131-142 (2003)
  213. α-Thalassemia associated with hb instability: a tale of two features. the case of Hb Rogliano or α1 Cod 108(G15)Thr→Asn and Hb Policoro or α2 Cod 124(H7)Ser→Pro. Bisconte MG, Caldora M, Musollino G, Cardiero G, Flagiello A, La Porta G, Lagona L, Prezioso R, Qualtieri G, Gaudiano C, Medulla E, Merlino A, Pucci P, Lacerra G. PLoS One 10 e0115738 (2015)
  214. A "living fossil" sequence: primary structure of the coelacanth (Latimeria chalumnae) hemoglobin--evolutionary and functional aspects. Gorr T, Kleinschmidt T, Sgouros JG, Kasang L. Biol Chem Hoppe Seyler 372 599-612 (1991)
  215. Allostery of the two-state model of hemoglobin studied by ECEPP energy minimization. Seno Y. J Comput Chem 27 701-710 (2006)
  216. Characterization of isomeric cationic porphyrins with beta-pyrrolic substituents by electrospray mass spectrometry: the singular behavior of a potential virus photoinactivator. Izquierdo RA, Barros CM, Santana-Marques MG, Ferrer-Correia AJ, Silva EM, Giuntini F, Faustino MA, Tomé JP, Tomé AC, Silva AM, Neves GP, Cavaleiro JA, Peixoto AF, Pereira MM, Pais AA. J Am Soc Mass Spectrom 18 218-225 (2007)
  217. Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution. Sutherland-Smith AJ, Baker HM, Hofmann OM, Brittain T, Baker EN. J Mol Biol 280 475-484 (1998)
  218. Entropy-driven intermediate steps of oxygenation may regulate the allosteric behavior of hemoglobin. Bucci E, Gryczynski Z, Razynska A, Kwansa H. Biophys J 74 2638-2648 (1998)
  219. Normal coordinate structural decomposition of the heme distortions of hemoglobin in various quaternary states and bound to allosteric effectors. Laberge M, Yonetani T, Fidy J. Mol Divers 7 15-23 (2003)
  220. Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect. Schweitzer-Stenner R, Bosenbeck M, Dreybrodt W. Biophys J 64 1194-1209 (1993)
  221. The primary structure of three hemoglobin chains from the indigo snake (Drymarchon corais erebennus, Serpentes): first evidence for alphaD chains and two beta chain types in snakes. Stoeckelhuber M, Gorr T, Kleinschmidt T. Biol Chem 383 1907-1916 (2002)
  222. Using the Tools and Resources of the RCSB Protein Data Bank. Costanzo LD, Ghosh S, Zardecki C, Burley SK. Curr Protoc Bioinformatics 55 1.9.1-1.9.35 (2016)
  223. mRNA Analysis of Frameshift Mutations with Stop Codon in the Last Exon: The Case of Hemoglobins Campania [α1 cod95 (-C)] and Sciacca [α1 cod109 (-C)]. Cardiero G, Musollino G, Prezioso R, Lacerra G. Biomedicines 9 1390 (2021)
  224. An alternative theoretical formula for hemoglobin oxygenation. Michel D. Eur Biophys J 37 823-827 (2008)
  225. Assessment of Cysteine Reactivity of Human Hemoglobin at Its Residue Level: A Mass Spectrometry-Based Approach. Mitra A, Muralidharan M, Srivastava D, Das R, Bhat V, Mandal AK. Hemoglobin 41 300-305 (2017)
  226. Characterization of hemoglobin Würzburg (alpha2beta2 4(A1)Thr-->Asn), a new electrophoretically silent variant, by mass spectrometry and molecular modeling studies. Bissé E, Zorn N, Boussert S, Epting T, Van Dorsselaer A, Horst J, Baumstark M, Wieland H. J Chromatogr A 1115 118-124 (2006)
  227. Crystallization of the rainbow trout (Salmo gairdneri) haemoglobin IV. Dodson GG, Richard VR, Tolley SP, Waller DA, Weber RE. J Mol Biol 211 691-692 (1990)
  228. Design, Synthesis, and Antisickling Investigation of a Nitric Oxide-Releasing Prodrug of 5HMF for the Treatment of Sickle Cell Disease. Alhashimi RT, Ghatge MS, Donkor AK, Deshpande TM, Anabaraonye N, Alramadhani D, Danso-Danquah R, Huang B, Zhang Y, Musayev FN, Abdulmalik O, Safo MK. Biomolecules 12 696 (2022)
  229. Effect of Mutations on mRNA and Globin Stability: The Cases of Hb Bernalda/Groene Hart and Hb Southern Italy. Cardiero G, Musollino G, Friscia MG, Testa R, Virruso L, Di Girgenti C, Caldora M, Colella Bisogno R, Gaudiano C, Manco G, Lacerra G. Genes (Basel) 11 E870 (2020)
  230. Effect of Occluded Ligand Migration on the Kinetics and Structural Dynamics of Homodimeric Hemoglobin. Kim H, Kim JG, Muniyappan S, Kim TW, Lee SJ, Ihee H. J Phys Chem B 124 1550-1556 (2020)
  231. Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin. Wajcman H, Kister J, Riou J, Galactéros F, Girot R, Maier-Redelsperger M, Nayudu NV, Giordano PC. Hemoglobin 22 11-22 (1998)
  232. Intermediate states in ligand photodissociation of carboxymyoglobin studies by dispersive X-ray absorption. Della Longa S D, Ascone I, Fontaine A, Congiu Castellano A, Bianconi A. Eur Biophys J 23 361-368 (1994)
  233. Iron distances in hemoglobin: comparison of x-ray crystallographic and extended x-ray absorption fine structure studies. Fermi G, Perutz MF, Shulman RG. Proc Natl Acad Sci U S A 84 6167-6168 (1987)
  234. Molecular modelling of Trematomus newnesi Hb 1: insights for a lowered oxygen affinity and lack of root effect. D'Avino R, De Luca R. Proteins 39 155-165 (2000)
  235. Probing the solution structure of tumor necrosis factor-α homotrimer and heterotrimer after complex perturbation using electrospray ionization mass spectrometry. Beil EJ, Heavner GA, Wu SJ, Nemeth JF. J Mol Recognit 25 174-183 (2012)
  236. Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin. Esquerra RM, Bibi BM, Tipgunlakant P, Birukou I, Soman J, Olson JS, Kliger DS, Goldbeck RA. Biochemistry 55 4005-4017 (2016)
  237. Stereospinomers of pentacoordinate iron porphyrin complexes: the case of the [Fe(porphyrinato)(CN)]- anions. Cirera J, Alvarez S. Dalton Trans 42 7002-7008 (2013)
  238. Study of the relationship of small variations of the molecular structure and the iron state in iron containing proteins by Mössbauer spectroscopy: biomedical approach. Oshtrakh MI. Spectrochim Acta A Mol Biomol Spectrosc 60 217-234 (2004)
  239. A new relaxed state in horse methemoglobin characterized by crystallographic studies. Sankaranarayanan R, Biswal BK, Vijayan M. Proteins 60 547-551 (2005)
  240. Activation of the low oxygen affinity-inducing potential of the Asn108(beta)-->Lys mutation of Hb-Presbyterian on intramolecular alpha alpha-fumaryl cross-bridging. Manjula BN, Malavalli A, Prabhakaran M, Friedman JM, Acharya AS. Protein Eng 14 359-366 (2001)
  241. Amino acid sequences of hemoglobin beta chains of five species of pinnipeds: Neophoca cinerea, Otaria byronia, Eumetopias jubatus, Pusa hispida, and Pagophilus groenlandica. Ikehara T, Eguchi Y, Kayo S, Takei H. J Protein Chem 15 659-665 (1996)
  242. Binding modes of L35 to alpha- and beta-semihemoglobins: structural insights into the inequivalence of alpha- and beta-subunits of hemoglobin. De Rosa MC, Carelli Alinovi C, Russo A, Giardina B. Biochem Biophys Res Commun 354 720-726 (2007)
  243. Binding of ibuprofen to human hemoglobin: elucidation of their molecular recognition by spectroscopy, calorimetry, and molecular modeling techniques. Seal P, Sikdar J, Roy A, Haldar R. J Biomol Struct Dyn 36 3137-3154 (2018)
  244. Comparative quantum-chemical analysis of the electronic structure and Mössbauer parameters of the active site models for deoxymyoglobin and alpha- and beta-subunits of tetrameric deoxyhemoglobin. Khleskov VI, Burykin BN, Smirnov AB, Oshtrakh MI. Biochem Biophys Res Commun 155 1255-1260 (1988)
  245. Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin. Ji X, Braxenthaler M, Moult J, Fronticelli C, Bucci E, Gilliland GL. Proteins 30 309-320 (1998)
  246. Does helix dipole have any role in binding metal ions in protein structures? Chakrabarti P. Arch Biochem Biophys 290 387-390 (1991)
  247. Hemoglobins with multiple reactive sulphydryl groups: the reaction of pigeon hemoglobin with 5,5'-dithiobis (2-nitrobenzoic acid). Okonjo KO, Okia TO. J Protein Chem 12 639-646 (1993)
  248. Indirect allosteric effects of a neutral mutation. Structure of deoxyhaemoglobin north Chicago (ProC2(36)beta----Ser). Perutz MF, Fermi G, Fogg J, Rahbar S. J Mol Biol 201 459-461 (1988)
  249. Location of potential binding sites on deoxy hemoglobin for the design of antigelling agents. Manavalan P, Prabhakaran M, Johnson ME. J Mol Biol 223 791-800 (1992)
  250. Mapping blood biochemistry by Raman spectroscopy at the cellular level. Volkov VV, McMaster J, Aizenberg J, Perry CC. Chem Sci 13 133-140 (2021)
  251. Max Perutz's achievements: how did he do it? Eisenberg D. Protein Sci 3 1625-1628 (1994)
  252. Mechanism Investigation of Wuwei Shexiang Pills on Gouty Arthritis via Network Pharmacology, Molecule Docking, and Pharmacological Verification. Lang J, Li L, Chen S, Quan Y, Yi J, Zeng J, Li Y, Zhao J, Yin Z. Evid Based Complement Alternat Med 2022 2377692 (2022)
  253. Modeling conformational change in macromolecules as an elastic deformation. Andrews LC, Harrison RW. Proteins 10 162-170 (1991)
  254. Molecular dynamics of sickle and normal hemoglobins. Prabhakaran M, Johnson ME. Biopolymers 33 735-742 (1993)
  255. Relative-residue surface-accessibility patterns reveal myoglobin and catalase similarity. Cockcroft VB, Osguthorpe DJ. FEBS Lett 293 149-152 (1991)
  256. Structural study and preliminary crystallographic data for the hemoglobin from reindeer (Rangifer tarandus tarandus) Conti E, Casale E, Ascenzi P, Coletta M, Condo SG, Merli A, Giardina B, Bordo D, Bolognesi M. Biochem Biophys Res Commun 187 1063-1070 (1992)
  257. Structure of deoxyhemoglobin: ionizable groups and polyethylene glycol. Saroff HA. Proteins 50 329-340 (2003)
  258. Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms. Balasubramanian M, Sathya Moorthy P, Neelagandan K, Ramadoss R, Kolatkar PR, Ponnuswamy MN. Acta Crystallogr D Biol Crystallogr 70 1898-1906 (2014)
  259. The Relationship between APOL1 Structure and Function: Clinical Implications. Madhavan SM, Buck M. Kidney360 2 134-140 (2021)
  260. The first sequenced normal hemoglobin lacking histidine in position 146 of the beta-chains. The primary structures of the major and minor hemoglobin components of the great crested newt (Triturus cristatus, Urodela, Amphibia). Kleinschmidt T, Sgouros JG, Braunitzer G. Biol Chem Hoppe Seyler 369 1343-1360 (1988)
  261. The primary structure of the hemoglobin of the Indian false vampire (Megaderma lyra, Microchiroptera). Sgouros JG, Kleinschmidt T, Braunitzer G. Biol Chem Hoppe Seyler 369 47-53 (1988)
  262. Thermal-induced force release in oxyhemoglobin. Gevorkian SG, Allahverdyan AE, Gevorgyan DS, Hu CK. Sci Rep 5 13064 (2015)
  263. XANES spectroscopy of carp hemoglobin-iron in correlation with the affinity changes of the protein for ligand. Pin S, Cortes R, Alpert B. FEBS Lett 208 325-330 (1986)
  264. Zinc finger nucleases for targeted mutagenesis and repair of the sickle-cell disease mutation: An in-silico study. Wayengera M. BMC Blood Disord 12 5 (2012)
  265. A Clinical Update of the Hb Siirt [β27(B9)Ala→Gly; HBB: c.83C>G] Hemoglobin Variant. Cappabianca MP, Colosimo A, Sabatucci A, Dainese E, Di Biagio P, Piscitelli R, Sarra O, Zei D, Amato A. Hemoglobin 41 53-55 (2017)
  266. Alteration of an intersubunit contact in hemoglobin variants: comparative study of modifications at position alpha 126 Asp (H9). Kister J, Griffon N, Henthorn JS, Marden MC, Poyart C, Papassotiriou I, Promé D, Galactéros F, Davies SC, Wajcman H. C R Acad Sci III 320 849-855 (1997)
  267. Characterization of a Tumor-Microenvironment-Relevant Gene Set Based on Tumor Severity in Colon Cancer and Evaluation of Its Potential for Dihydroartemisinin Targeting. Liang B, Zheng B, Zhou Y, Lai ZQ, Zhang C, Yan Z, Li Z, Li X, Gong P, Qu J, Liu J. Evid Based Complement Alternat Med 2021 4812068 (2021)
  268. Computational Insight on the Interaction of Common Blood Proteins with Gold Nanoparticles. Tavanti F, Menziani MC. Int J Mol Sci 22 8722 (2021)
  269. Cross-linking hemoglobin by design: lessons from using molecular clamps. Kluger R, Jones RT, Shih DT. Artif Cells Blood Substit Immobil Biotechnol 22 415-428 (1994)
  270. Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans. Sundaresan SS, Ramesh P, Shobana N, Vinuchakkaravarthy T, Yasien S, Ponnuswamy MNG. Acta Crystallogr F Struct Biol Commun 77 113-120 (2021)
  271. Effect of the tertiary structure alteration by ligation on the interface contacts between subunits of hemoglobin. Arata Y. Biochim Biophys Acta 1247 24-34 (1995)
  272. Feed-forward neural networks for secondary structure prediction. Barlow TW. J Mol Graph 13 175-183 (1995)
  273. Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain silent variant in a family with multiple Hb disorders. Deutsch S, Darbellay R, Offord R, Frutiger A, Kister J, Wajcman H, Beris P. Am J Hematol 61 187-193 (1999)
  274. Modeling microdomains: the surface area of globin helices. Weaver DL. Proteins 13 327-335 (1992)
  275. Movements at the hemoglobin A-hemes and their role in ligand binding, analyzed by X-ray crystallography. Dodson E, Dodson G. Biopolymers 91 1056-1063 (2009)
  276. NMR characterization of a diamagnetic model of unliganded alpha chains from human hemoglobin. Martineau L, Pagnier J, Mispelter J, Craescu CT. Biochimie 74 845-851 (1992)
  277. Optimism, persistence, and our collective crystal ball. Wellems TE. Am J Trop Med Hyg 83 1-6 (2010)
  278. Simple dimer containing dissociatively stable mono-imidazole ligated ferrohemes. Yang QZ, Khvostichenko D, Atkinson JD, Boulatov R. Chem Commun (Camb) 963-965 (2008)
  279. Structural and Functional Characterization of a New Double Variant Haemoglobin (HbG-Philadelphia/Duarte α(2)β(2)). Fais A, Casu M, Ruggerone P, Ceccarelli M, Porcu S, Era B, Anedda R, Sollaino MC, Galanello R, Corda M. ISRN Hematol 2011 735314 (2011)
  280. Synchrotron Radiation as a Tool for Macromolecular X-Ray Crystallography: a XXI Century Perspective. Grabowski M, Cooper DR, Brzezinski D, Macnar JM, Shabalin IG, Cymborowski M, Otwinowski Z, Minor W. Nucl Instrum Methods Phys Res B 489 30-40 (2021)
  281. The hemoglobins of the "fossil fish" Acipenser naccarii: functional properties and their structural basis. Clementi ME, De Rosa MC, Bertonati C, Capo C, Cataldi E, Petruzzelli R, Giardina B. Hemoglobin 25 447-451 (2001)
  282. Tyrosyl radical in haemoglobin and haptoglobin-haemoglobin complex: how does haptoglobin make haemoglobin less toxic? Svistunenko DA, Manole A. J Biomed Res 34 281-291 (2019)
  283. [Molecular engineering of hemoglobin for transfusion]. Poyart C, Baudin V, Pagnier J. Rev Fr Transfus Hemobiol 35 417-424 (1992)
  284. Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region. Oshima M, Nakamura S, Atassi MZ. J Protein Chem 12 403-412 (1993)
  285. Carnivora: the primary structure of the beach marten (Martes foina, Mustelidae) hemoglobin. Rücknagel KP, Wiesner H, Braunitzer G. Biol Chem Hoppe Seyler 371 503-509 (1990)
  286. Characteristic of aromatic amino acid substitution at alpha 96 of hemoglobin. Choi JW, Lee JH, Lee KH, Lee HW, Sohn JH, Yoon JH, Yeh BI, Park SK, Lee KJ, Kim HW. J Biochem Mol Biol 38 115-119 (2005)
  287. Durene-capped porphyrin complexes of iron(II). Binding of imidazoles, and spectroscopic trends within Fe(porp)B(L) species (B = imidazole base; L = RNC, CO, O2). David S, James BR, Dolphin D. J Inorg Biochem 28 125-135 (1986)
  288. Effect of aromatic isothiocyanates on the functional properties of human hemoglobin. Role of the stereochemistry of the charged group. Ippoliti R, Currell D, Lendaro E, Bellelli A, Castagnola M, Bolognesi M, Brunori M. Biophys Chem 37 293-302 (1990)
  289. Effect of toxic ligands on O2 binding to heme and their toxicity mechanism. Li R, Dai X, Feng Z, Li Y, Zhao M, Liu J, Li H, Chen Y, Ma Y, Tang Y. Phys Chem Chem Phys 21 14957-14963 (2019)
  290. Exploring the mechanism of Suanzaoren decoction in treatment of insomnia based on network pharmacology and molecular docking. Wang S, Zhao Y, Hu X. Front Pharmacol 14 1145532 (2023)
  291. Haemoglobin(βK120C)-albumin trimer as an artificial O2 carrier with sufficient haemoglobin allostery. Morita Y, Saito A, Yamaguchi J, Komatsu T. RSC Chem Biol 1 128-136 (2020)
  292. Identifiability of equilibrium constants for receptors with two to five binding sites. Benndorf K, Schulz E. J Gen Physiol 155 e202313423 (2023)
  293. Influence of mutations at the proximal histidine position on the Fe-O2 bond in hemoglobin from density functional theory. Todde G, Hovmöller S, Laaksonen A. J Chem Phys 144 095101 (2016)
  294. Mitochondrial Haemoglobin Is Upregulated with Hypoxia in Skeletal Muscle and Has a Conserved Interaction with ATP Synthase and Inhibitory Factor 1. Ebanks B, Katyal G, Taylor C, Dowle A, Papetti C, Lucassen M, Moisoi N, Chakrabarti L. Cells 12 912 (2023)
  295. Molecular modeling and small angle X-ray scattering studies of Hoplosternum littorale cathodic haemoglobin. Peres P, Lombardi FR, Dos Santos GC, Olivieri JR, Canduri F, Bonilla-Rodriguez GO, de Azevedo WF. Biochem Biophys Res Commun 325 487-493 (2004)
  296. Nitrite Reductase Activity of Ferrous Nitrobindins: A Comparative Study. De Simone G, di Masi A, Tundo GR, Coletta M, Ascenzi P. Int J Mol Sci 24 6553 (2023)
  297. Sequential assignment of proton resonances in the NMR spectrum of Zn-substituted alpha chains from human hemoglobin. Ligand-induced tertiary changes in the heme pocket. Martineau L, Craescu CT. Eur J Biochem 214 383-393 (1993)
  298. Single-Molecule X-ray Scattering Used to Visualize the Conformation Distribution of Biological Molecules via Single-Object Scattering Sampling. Lee S, Ki H, Lee SJ, Ihee H. Int J Mol Sci 24 17135 (2023)
  299. Site-specific semisynthetic variant of human hemoglobin. Hefta SA, Lyle SB, Busch MR, Harris DE, Matthew JB, Gurd FR. Proc Natl Acad Sci U S A 85 709-713 (1988)
  300. Structural studies on a low oxygen affinity hemoglobin from mammalian species: sheep (Ovis aries). Kamariah N, Ponnuraj SM, Moovarkumudalvan B, Ponnuswamy MN. Biochem Biophys Res Commun 450 36-41 (2014)
  301. Symmetry distortion in the human hemoglobin tetramer induced by asymmetric ligation. Shibayama N. FEBS Lett 586 74-78 (2012)
  302. Synchrotron science in the UK: NINA, the SRS and Diamond. Hasnain SS, Catlow CRA. Philos Trans A Math Phys Eng Sci 377 20190147 (2019)
  303. The primary structure of the hemoglobin from the Australian ghost bat (Macroderma gigas, Microchiroptera). Singer GA, Kleinschmidt T, Pettigrew JD, Braunitzer G. Biol Chem Hoppe Seyler 372 1089-1095 (1991)


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  1. Stereochemistry of Iron in Deoxyhaemoglobin. Perutz MF, Hasnain SS, Duke PJ, Sessler JL, Hahn JE Nature 295 535- (1982)
  2. . Fermi G, Perutz MF Haemoglobin and Myoglobin. Atlas of Molecular Structures in Biology 2 - (1981)
  3. Regulation of Oxygen Affinity of Hemoglobin. Influence of Structure of the Globin on the Heme Iron. Perutz MF Annu. Rev. Biochem. 48 327- (1979)
  4. Three-Dimensional Fourier Synthesis of Human Deoxyhemoglobin at 2.5 Angstroms Resolution, I.X-Ray Analysis. Teneyck LF, Arnone A J. Mol. Biol. 100 3- (1976)
  5. Three-Dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 2.5 Angstroms Resolution, Refinement of the Atomic Model. Fermi G J. Mol. Biol. 97 237- (1975)
  6. Three-Dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 3.5 Angstroms Resolution. Muirhead H, Greer J Nature 228 516- (1970)