PDBsum entry 4hhb

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Oxygen transport PDB id
Jmol PyMol
Protein chains
141 a.a. *
146 a.a. *
HEM ×4
PO4 ×2
Waters ×221
* Residue conservation analysis
PDB id:
Name: Oxygen transport
Title: The crystal structure of human deoxyhaemoglobin at 1.74 angs resolution
Structure: Hemoglobin (deoxy) (alpha chain). Chain: a, c. Engineered: yes. Hemoglobin (deoxy) (beta chain). Chain: b, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Biol. unit: Tetramer (from PQS)
1.74Å     R-factor:   0.135    
Authors: G.Fermi,M.F.Perutz
Key ref:
G.Fermi et al. (1984). The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. J Mol Biol, 175, 159-174. PubMed id: 6726807 DOI: 10.1016/0022-2836(84)90472-8
07-Mar-84     Release date:   17-Jul-84    
Supersedes: 1hhb
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P69905  (HBA_HUMAN) -  Hemoglobin subunit alpha
142 a.a.
141 a.a.
Protein chains
Pfam   ArchSchema ?
P68871  (HBB_HUMAN) -  Hemoglobin subunit beta
147 a.a.
146 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   11 terms 
  Biological process     transport   17 terms 
  Biochemical function     protein binding     9 terms  


DOI no: 10.1016/0022-2836(84)90472-8 J Mol Biol 175:159-174 (1984)
PubMed id: 6726807  
The crystal structure of human deoxyhaemoglobin at 1.74 A resolution.
G.Fermi, M.F.Perutz, B.Shaanan, R.Fourme.
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.
  Selected figure(s)  
Figure 1.
FG2, FG4 /I1 CD2, CD3, FG2, FG4, haem fi, CD5, CD8, D7, El-E3 a,
Figure 3.
I'he 3.4 (4) 111: I' 1%~ > 44 3.x (4) His 3.2 (9) 1: K Hi,
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1984, 175, 159-174) copyright 1984.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21256216 F.Arisaka, Y.Nagai, and M.Nagai (2011).
Dimer-tetramer association equilibria of human adult hemoglobin and its mutants as observed by analytical ultracentrifugation.
  Methods, 54, 175-180.  
21240532 H.J.Nothnagel, M.R.Preimesberger, M.P.Pond, B.Y.Winer, E.M.Adney, and J.T.Lecomte (2011).
Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.
  J Biol Inorg Chem, 16, 539-552.  
22199401 R.J.Gildea, L.J.Bourhis, O.V.Dolomanov, R.W.Grosse-Kunstleve, H.Puschmann, P.D.Adams, and J.A.Howard (2011).
iotbx.cif: a comprehensive CIF toolbox.
  J Appl Crystallogr, 44, 1259-1263.  
21415366 S.Fischer, K.W.Olsen, K.Nam, and M.Karplus (2011).
Unsuspected pathway of the allosteric transition in hemoglobin.
  Proc Natl Acad Sci U S A, 108, 5608-5613.  
20661989 F.E.Lui, and R.Kluger (2010).
Reviving artificial blood: meeting the challenge of dealing with NO scavenging by hemoglobin.
  Chembiochem, 11, 1816-1824.  
19846609 J.Binkley, K.Karra, A.Kirby, M.Hosobuchi, E.A.Stone, and A.Sidow (2010).
ProPhylER: a curated online resource for protein function and structure based on evolutionary constraint analyses.
  Genome Res, 20, 142-154.  
20680411 J.D.Méndez, J.Xie, M.Aguilar-Hernández, and V.Méndez-Valenzuela (2010).
Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases.
  Mol Cell Biochem, 344, 185-193.  
20463873 J.S.Hub, M.B.Kubitzki, and Groot (2010).
Spontaneous quaternary and tertiary T-R transitions of human hemoglobin in molecular dynamics simulation.
  PLoS Comput Biol, 6, e1000774.  
20668762 R.M.Esquerra, I.López-Peña, P.Tipgunlakant, I.Birukou, R.L.Nguyen, J.Soman, J.S.Olson, D.S.Kliger, and R.A.Goldbeck (2010).
Kinetic spectroscopy of heme hydration and ligand binding in myoglobin and isolated hemoglobin chains: an optical window into heme pocket water dynamics.
  Phys Chem Chem Phys, 12, 10270-10278.  
20595466 T.E.Wellems (2010).
Optimism, persistence, and our collective crystal ball.
  Am J Trop Med Hyg, 83, 1-6.  
19353640 E.Dodson, and G.Dodson (2009).
Movements at the hemoglobin A-hemes and their role in ligand binding, analyzed by X-ray crystallography.
  Biopolymers, 91, 1056-1063.  
19267450 L.J.Juszczak, and R.Z.Desamero (2009).
Extension of the tryptophan chi2,1 dihedral angle-W3 band frequency relationship to a full rotation: correlations and caveats.
  Biochemistry, 48, 2777-2787.  
18286275 D.Michel (2008).
An alternative theoretical formula for hemoglobin oxygenation.
  Eur Biophys J, 37, 823-827.  
18578646 J.F.Storz, and H.Moriyama (2008).
Mechanisms of hemoglobin adaptation to high altitude hypoxia.
  High Alt Med Biol, 9, 148-157.  
18806790 M.Cammarata, M.Levantino, F.Schotte, P.A.Anfinrud, F.Ewald, J.Choi, A.Cupane, M.Wulff, and H.Ihee (2008).
Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.
  Nat Methods, 5, 881-886.  
18096633 M.Laberge, and T.Yonetani (2008).
Molecular dynamics simulations of hemoglobin A in different states and bound to DPG: effector-linked perturbation of tertiary conformations and HbA concerted dynamics.
  Biophys J, 94, 2737-2751.  
18785728 P.Cozzini, G.E.Kellogg, F.Spyrakis, D.J.Abraham, G.Costantino, A.Emerson, F.Fanelli, H.Gohlke, L.A.Kuhn, G.M.Morris, M.Orozco, T.A.Pertinhez, M.Rizzi, and C.A.Sotriffer (2008).
Target flexibility: an emerging consideration in drug discovery and design.
  J Med Chem, 51, 6237-6255.  
  18540052 P.S.Kaushal, R.Sankaranarayanan, and M.Vijayan (2008).
Water-mediated variability in the structure of relaxed-state haemoglobin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 463-469.
PDB codes: 2zlt 2zlu 2zlv 2zlw 2zlx
18283350 Q.Z.Yang, D.Khvostichenko, J.D.Atkinson, and R.Boulatov (2008).
Simple dimer containing dissociatively stable mono-imidazole ligated ferrohemes.
  Chem Commun (Camb), (), 963-965.  
18359768 R.M.Esquerra, R.A.Jensen, S.Bhaskaran, M.L.Pillsbury, J.L.Mendoza, B.W.Lintner, D.S.Kliger, and R.A.Goldbeck (2008).
The pH dependence of heme pocket hydration and ligand rebinding kinetics in photodissociated carbonmonoxymyoglobin.
  J Biol Chem, 283, 14165-14175.  
18376851 X.J.Song, V.Simplaceanu, N.T.Ho, and C.Ho (2008).
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.
  Biochemistry, 47, 4907-4915.  
17664960 A.Charvat, and B.Abel (2007).
How to make big molecules fly out of liquid water: applications, features and physics of laser assisted liquid phase dispersion mass spectrometry.
  Phys Chem Chem Phys, 9, 3335-3360.  
17393459 I.N.Kasampalidis, I.Pitas, and K.Lyroudia (2007).
Conservation of metal-coordinating residues.
  Proteins, 68, 123-130.  
18075577 J.Kuriyan, and D.Eisenberg (2007).
The origin of protein interactions and allostery in colocalization.
  Nature, 450, 983-990.  
17279499 M.Saito, and I.Okazaki (2007).
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.
  J Comput Chem, 28, 1129-1136.  
17381072 P.Nacharaju, J.M.Friedman, M.Prabhakaran, S.A.Acharya, and B.N.Manjula (2007).
Combining the influence of two low O2 affinity-inducing chemical modifications of the central cavity of hemoglobin.
  Biochemistry, 46, 4554-4564.  
17070697 R.A.Izquierdo, C.M.Barros, M.G.Santana-Marques, A.J.Ferrer-Correia, E.M.Silva, F.Giuntini, M.A.Faustino, J.P.Tomé, A.C.Tomé, A.M.Silva, G.P.Neves, J.A.Cavaleiro, A.F.Peixoto, M.M.Pereira, and A.A.Pais (2007).
Characterization of isomeric cationic porphyrins with beta-pyrrolic substituents by electrospray mass spectrometry: the singular behavior of a potential virus photoinactivator.
  J Am Soc Mass Spectrom, 18, 218-225.  
17691822 S.C.Sahu, V.Simplaceanu, Q.Gong, N.T.Ho, F.Tian, J.H.Prestegard, and C.Ho (2007).
Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector.
  Biochemistry, 46, 9973-9980.  
17973182 S.Srinivasulu, A.S.Acharya, M.Prabhakaran, M.E.Fabry, R.Alami, S.N.Fiering, E.E.Bouhasirra, and R.L.Nagel (2007).
HbS-Savaria: the anti-polymerization effect of a single mutation in human alpha-chains.
  Protein J, 26, 523-532.  
17372357 T.J.Oldfield (2007).
CAALIGN: a program for pairwise and multiple protein-structure alignment.
  Acta Crystallogr D Biol Crystallogr, 63, 514-525.  
17497935 X.J.Song, Y.Yuan, V.Simplaceanu, S.C.Sahu, N.T.Ho, and C.Ho (2007).
A comparative NMR study of the polypeptide backbone dynamics of hemoglobin in the deoxy and carbonmonoxy forms.
  Biochemistry, 46, 6795-6803.  
16845667 E.Podstawka, P.J.Mak, J.R.Kincaid, and L.M.Proniewicz (2006).
Low frequency resonance Raman spectra of isolated alpha and beta subunits of hemoglobin and their deuterated analogues.
  Biopolymers, 83, 455-466.  
16807972 J.D.Maréchal, F.Maseras, A.Lledós, L.Mouawad, and D.Perahia (2006).
A DFT study on the relative affinity for oxygen of the alpha and beta subunits of hemoglobin.
  J Comput Chem, 27, 1446-1453.  
16684887 J.E.Knapp, R.Pahl, V.Srajer, and W.E.Royer (2006).
Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin.
  Proc Natl Acad Sci U S A, 103, 7649-7654.
PDB codes: 2grf 2grh 2grz
16782791 P.J.Kundrotas, and E.Alexov (2006).
Electrostatic properties of protein-protein complexes.
  Biophys J, 91, 1724-1736.  
16514594 Y.Seno (2006).
Allostery of the two-state model of hemoglobin studied by ECEPP energy minimization.
  J Comput Chem, 27, 701-710.  
15847586 B.R.Wood, L.Hammer, L.Davis, and D.McNaughton (2005).
Raman microspectroscopy and imaging provides insights into heme aggregation and denaturation within human erythrocytes.
  J Biomed Opt, 10, 14005.  
15922591 J.T.Lecomte, D.A.Vuletich, and A.M.Lesk (2005).
Structural divergence and distant relationships in proteins: evolution of the globins.
  Curr Opin Struct Biol, 15, 290-301.  
15475581 K.Victor, A.Van-Quynh, and R.G.Bryant (2005).
High frequency dynamics in hemoglobin measured by magnetic relaxation dispersion.
  Biophys J, 88, 443-454.  
15858266 L.N.Patskovska, Y.V.Patskovsky, S.C.Almo, and R.E.Hirsch (2005).
COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000.
  Acta Crystallogr D Biol Crystallogr, 61, 566-573.
PDB codes: 1m9p 1nej
15822103 R.A.Boykins, P.W.Buehler, Y.Jia, R.Venable, and A.I.Alayash (2005).
O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: structural and functional consequences of beta93Cys modification.
  Proteins, 59, 840-855.  
15887226 R.Sankaranarayanan, B.K.Biswal, and M.Vijayan (2005).
A new relaxed state in horse methemoglobin characterized by crystallographic studies.
  Proteins, 60, 547-551.
PDB codes: 1y8h 1y8i 1y8k
15573374 S.M.Vaiana, M.A.Rotter, A.Emanuele, F.A.Ferrone, and M.B.Palma-Vittorelli (2005).
Effect of T-R conformational change on sickle-cell hemoglobin interactions and aggregation.
  Proteins, 58, 426-438.  
15932877 W.E.Royer, H.Zhu, T.A.Gorr, J.F.Flores, and J.E.Knapp (2005).
Allosteric hemoglobin assembly: diversity and similarity.
  J Biol Chem, 280, 27477-27480.  
14699100 L.J.Deterding, D.C.Ramirez, J.R.Dubin, R.P.Mason, and K.B.Tomer (2004).
Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical.
  J Biol Chem, 279, 11600-11607.  
15096632 S.Srinivasulu, B.N.Manjula, R.L.Nagel, C.H.Tsai, C.Ho, M.Prabhakaran, and S.A.Acharya (2004).
Hemoglobin Einstein: semisynthetic deletion in the B-helix of the alpha-chain.
  Protein Sci, 13, 1266-1275.  
12773618 S.Adachi, S.Y.Park, J.R.Tame, Y.Shiro, and N.Shibayama (2003).
Direct observation of photolysis-induced tertiary structural changes in hemoglobin.
  Proc Natl Acad Sci U S A, 100, 7039-7044.
PDB codes: 1j3y 1j3z 1j40 1j41
11847280 A.Heifetz, E.Katchalski-Katzir, and M.Eisenstein (2002).
Electrostatics in protein-protein docking.
  Protein Sci, 11, 571-587.  
12093902 A.Riccio, L.Vitagliano, G.di Prisco, A.Zagari, and L.Mazzarella (2002).
The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.
  Proc Natl Acad Sci U S A, 99, 9801-9806.
PDB code: 1la6
12077435 B.K.Biswal, and M.Vijayan (2002).
Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state.
  Acta Crystallogr D Biol Crystallogr, 58, 1155-1161.
PDB codes: 1jy7 1lfl 1lfq 1lft 1lfv 1lfy 1lfz
12012442 B.R.Wood, and D.McNaughton (2002).
Micro-Raman characterization of high- and low-spin heme moieties within single living erythrocytes.
  Biopolymers, 67, 259-262.  
11969426 C.K.Chang, V.Simplaceanu, and C.Ho (2002).
Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces.
  Biochemistry, 41, 5644-5655.  
12118003 C.Verde, V.Carratore, A.Riccio, M.Tamburrini, E.Parisi, and G.Di Prisco (2002).
The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor.
  J Biol Chem, 277, 36312-36320.  
12239340 D.D.Klug, M.Z.Zgierski, J.S.Tse, Z.Liu, J.R.Kincaid, K.Czarnecki, and R.J.Hemley (2002).
Doming modes and dynamics of model heme compounds.
  Proc Natl Acad Sci U S A, 99, 12526-12530.  
12023247 L.Mouawad, D.Perahia, C.H.Robert, and C.Guilbert (2002).
New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations.
  Biophys J, 82, 3224-3245.  
11914488 M.K.Safo, T.Boyiri, J.C.Burnett, R.Danso-Danquah, C.M.Moure, G.S.Joshi, and D.J.Abraham (2002).
X-ray crystallographic analyses of symmetrical allosteric effectors of hemoglobin: compounds designed to link primary and secondary binding sites.
  Acta Crystallogr D Biol Crystallogr, 58, 634-644.
PDB code: 1k0y
12553727 M.Stoeckelhuber, T.Gorr, and T.Kleinschmidt (2002).
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.
  Biol Chem, 383, 1907-1916.  
12146965 S.Nagatomo, M.Nagai, N.Shibayama, and T.Kitagawa (2002).
Differences in changes of the alpha1-beta2 subunit contacts between ligand binding to the alpha and beta subunits of hemoglobin A: UV resonance raman analysis using Ni-Fe hybrid hemoglobin.
  Biochemistry, 41, 10010-10020.  
12095481 T.Brittain (2002).
Molecular aspects of embryonic hemoglobin function.
  Mol Aspects Med, 23, 293-342.  
11742119 T.Yagami, B.T.Ballard, J.C.Padovan, B.T.Chait, A.M.Popowicz, and J.M.Manning (2002).
N-terminal contributions of the gamma-subunit of fetal hemoglobin to its tetramer strength: remote effects at subunit contacts.
  Protein Sci, 11, 27-35.  
11566768 A.Riccio, M.Tamburrini, B.Giardina, and G.di Prisco (2001).
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?
  Biophys J, 81, 1938-1946.  
11151007 J.C.Burnett, P.Botti, D.J.Abraham, and G.E.Kellogg (2001).
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.
  Proteins, 42, 355-377.  
11316875 M.K.Safo, C.M.Moure, J.C.Burnett, G.S.Joshi, and D.J.Abraham (2001).
High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector.
  Protein Sci, 10, 951-957.
PDB code: 1g9v
11369847 M.K.Safo, and D.J.Abraham (2001).
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.
  Protein Sci, 10, 1091-1099.
PDB code: 1fsx
11391770 M.R.Mihailescu, C.Fronticelli, and I.M.Russu (2001).
Allosteric free energy changes at the alpha 1 beta 2 interface of human hemoglobin probed by proton exchange of Trp beta 37.
  Proteins, 44, 73-78.  
11606302 R.A.Goldbeck, S.J.Paquette, and D.S.Kliger (2001).
The effect of water on the rate of conformational change in protein allostery.
  Biophys J, 81, 2919-2934.  
11375530 R.D.Kidd, A.Mathews, H.M.Baker, T.Brittain, and E.N.Baker (2001).
Subunit dissociation and reassociation leads to preferential crystallization of haemoglobin Bart's (gamma4) from solutions of human embryonic haemoglobin Portland (zeta2gamma2) at low pH.
  Acta Crystallogr D Biol Crystallogr, 57, 921-924.  
11514664 R.D.Kidd, H.M.Baker, A.J.Mathews, T.Brittain, and E.N.Baker (2001).
Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia.
  Protein Sci, 10, 1739-1749.
PDB codes: 1i3d 1i3e
11343922 W.E.Royer, J.E.Knapp, K.Strand, and H.A.Heaslet (2001).
Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms.
  Trends Biochem Sci, 26, 297-304.  
10930828 E.A.Brucker (2000).
Genetically crosslinked hemoglobin: a structural study.
  Acta Crystallogr D Biol Crystallogr, 56, 812-816.
PDB codes: 1c7b 1c7c 1c7d
10962034 J.A.Lukin, V.Simplaceanu, M.Zou, N.T.Ho, and C.Ho (2000).
NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin.
  Proc Natl Acad Sci U S A, 97, 10354-10358.  
10677211 J.C.Burnett, G.E.Kellogg, and D.J.Abraham (2000).
Computational methodology for estimating changes in free energies of biomolecular association upon mutation. The importance of bound water in dimer-tetramer assembly for beta 37 mutant hemoglobins.
  Biochemistry, 39, 1622-1633.  
10707029 J.D.Szustakowski, and Z.Weng (2000).
Protein structure alignment using a genetic algorithm.
  Proteins, 38, 428-440.  
10930827 J.R.Tame, and B.Vallone (2000).
The structures of deoxy human haemoglobin and the mutant Hb Tyralpha42His at 120 K.
  Acta Crystallogr D Biol Crystallogr, 56, 805-811.
PDB codes: 1a3n 1a3o
10771432 J.Wilson, and P.Main (2000).
The use of wavelet transforms in low-resolution phase extension.
  Acta Crystallogr D Biol Crystallogr, 56, 625-633.  
10986467 M.S.Hargrove, E.A.Brucker, B.Stec, G.Sarath, R.Arredondo-Peter, R.V.Klucas, J.S.Olson, and G.N.Phillips (2000).
Crystal structure of a nonsymbiotic plant hemoglobin.
  Structure, 8, 1005-1014.
PDB code: 1d8u
10998071 M.Tamburrini, A.Riccio, M.Romano, B.Giardina, and G.di Prisco (2000).
Structural and functional analysis of the two haemoglobins of the antarctic seabird Catharacta maccormicki characterization of an additional phosphate binding site by molecular modelling.
  Eur J Biochem, 267, 6089-6098.  
10737936 R.D'Avino, and R.De Luca (2000).
Molecular modelling of Trematomus newnesi Hb 1: insights for a lowered oxygen affinity and lack of root effect.
  Proteins, 39, 155-165.  
10790192 R.Li, Y.Nagai, and M.Nagai (2000).
Contribution of alpha140Tyr and beta37Trp to the near-UV CD spectra on quaternary structure transition of human hemoglobin A.
  Chirality, 12, 216-220.  
11112521 T.C.Mueser, P.H.Rogers, and A.Arnone (2000).
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin.
  Biochemistry, 39, 15353-15364.
PDB codes: 1g08 1g09 1g0a 1g0b
10713517 T.H.Lu, K.Panneerselvam, Y.C.Liaw, P.Kan, and C.J.Lee (2000).
Structure determination of porcine haemoglobin.
  Acta Crystallogr D Biol Crystallogr, 56, 304-312.
PDB code: 1qpw
11076510 T.Y.Fang, V.Simplaceanu, C.H.Tsai, N.T.Ho, and C.Ho (2000).
An additional H-bond in the alpha 1 beta 2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (beta L105W).
  Biochemistry, 39, 13708-13718.  
10920044 V.Simplaceanu, J.A.Lukin, T.Y.Fang, M.Zou, N.T.Ho, and C.Ho (2000).
Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin.
  Biophys J, 79, 1146-1154.  
10037733 J.E.Knapp, M.A.Oliveira, Q.Xie, S.R.Ernst, A.F.Riggs, and M.L.Hackert (1999).
The structural and functional analysis of the hemoglobin D component from chicken.
  J Biol Chem, 274, 6411-6420.
PDB code: 1hbr
10500299 J.R.Tame (1999).
What is the true structure of liganded haemoglobin?
  Trends Biochem Sci, 24, 372-377.  
10393295 K.T.Chong, G.Miyazaki, H.Morimoto, Y.Oda, and S.Y.Park (1999).
Structures of the deoxy and CO forms of haemoglobin from Dasyatis akajei, a cartilaginous fish.
  Acta Crystallogr D Biol Crystallogr, 55, 1291-1300.
PDB codes: 1cg5 1cg8
10350458 L.A.Dick, G.Heibel, E.G.Moore, and T.G.Spiro (1999).
UV resonance Raman spectra reveal a structural basis for diminished proton and CO2 binding to alpha,alpha-cross-linked hemoglobin.
  Biochemistry, 38, 6406-6410.  
10521410 L.J.Juszczak, and J.M.Friedman (1999).
UV resonance raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin.
  J Biol Chem, 274, 30357-30360.  
10075661 R.Makino, H.Matsuda, E.Obayashi, Y.Shiro, T.Iizuka, and H.Hori (1999).
EPR characterization of axial bond in metal center of native and cobalt-substituted guanylate cyclase.
  J Biol Chem, 274, 7714-7723.  
10398311 S.Deutsch, R.Darbellay, R.Offord, A.Frutiger, J.Kister, H.Wajcman, and P.Beris (1999).
Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain silent variant in a family with multiple Hb disorders.
  Am J Hematol, 61, 187-193.  
10233060 S.E.Harding, J.C.Horton, S.Jones, J.M.Thornton, and D.J.Winzor (1999).
COVOL: an interactive program for evaluating second virial coefficients from the triaxial shape or dimensions of rigid macromolecules.
  Biophys J, 76, 2432-2438.  
10464287 V.Baudin-Creuza, C.Vasseur-Godbillon, N.Griffon, J.Kister, L.Kiger, C.Poyart, M.C.Marden, and J.Pagnier (1999).
Additive effects of beta chain mutations in low oxygen affinity hemoglobin betaF41Y,K66T.
  J Biol Chem, 274, 25550-25554.  
10090732 X.Hu, K.R.Rodgers, I.Mukerji, and T.G.Spiro (1999).
New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin kempsey.
  Biochemistry, 38, 3462-3467.  
9830011 D.J.Harrington, K.Adachi, and W.E.Royer (1998).
Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber.
  J Biol Chem, 273, 32690-32696.
PDB code: 6hbw
9665699 D.Wang, and T.G.Spiro (1998).
Structure changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopy.
  Biochemistry, 37, 9940-9951.  
9591687 E.Bucci, Z.Gryczynski, A.Razynska, and H.Kwansa (1998).
Entropy-driven intermediate steps of oxygenation may regulate the allosteric behavior of hemoglobin.
  Biophys J, 74, 2638-2648.  
9521755 E.S.Peterson, and J.M.Friedman (1998).
A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.
  Biochemistry, 37, 4346-4357.  
9692324 F.Nastri, A.Lombardi, L.D.D'Andrea, M.Sanseverino, O.Maglio, and V.Pavone (1998).
Miniaturized hemoproteins.
  Biopolymers, 47, 5.  
9761903 G.B.Vásquez, X.Ji, C.Fronticelli, and G.L.Gilliland (1998).
Human carboxyhemoglobin at 2.2 A resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins.
  Acta Crystallogr D Biol Crystallogr, 54, 355-366.
PDB code: 1aj9
  9494044 H.Wajcman, J.Kister, J.Riou, F.Galactéros, R.Girot, M.Maier-Redelsperger, N.V.Nayudu, and P.C.Giordano (1998).
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.
  Hemoglobin, 22, 11-22.  
9585529 K.Sudhakar, M.Laberge, A.Tsuneshige, and J.M.Vanderkooi (1998).
Zinc-substituted hemoglobins: alpha- and beta-chain differences monitored by high-resolution emission spectroscopy.
  Biochemistry, 37, 7177-7184.  
9760237 M.Marta, M.Patamia, A.Colella, S.Sacchi, M.Pomponi, K.M.Kovacs, C.Lydersen, and B.Giardina (1998).
Anionic binding site and 2,3-DPG effect in bovine hemoglobin.
  Biochemistry, 37, 14024-14029.  
9843411 N.L.Chan, P.H.Rogers, and A.Arnone (1998).
Crystal structure of the S-nitroso form of liganded human hemoglobin.
  Biochemistry, 37, 16459-16464.
PDB code: 1buw
9649327 X.Hu, L.A.Dick, and T.G.Spiro (1998).
Fourier transform infrared evidence against Asp beta 99 protonation in hemoglobin: nature of the Tyr alpha 42-Asp beta 99 quaternary H-bond.
  Biochemistry, 37, 9445-9448.  
9517546 X.Ji, M.Braxenthaler, J.Moult, C.Fronticelli, E.Bucci, and G.L.Gilliland (1998).
Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin.
  Proteins, 30, 309-320.  
9649306 Y.A.Puius, M.Zou, N.T.Ho, C.Ho, and S.C.Almo (1998).
Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp).
  Biochemistry, 37, 9258-9265.
PDB codes: 1rvw 1vwt
9099713 A.A.Komar, A.Kommer, I.A.Krasheninnikov, and A.S.Spirin (1997).
Cotranslational folding of globin.
  J Biol Chem, 272, 10646-10651.  
9132010 J.G.Pearson, B.Montez, H.Le, E.Oldfield, E.Y.Chien, and S.G.Sligar (1997).
Assignment and analysis of fluorine nuclear magnetic resonance spectra of 4-fluorotryptophan myoglobins and hemoglobins.
  Biochemistry, 36, 3590-3599.  
9499936 J.Kister, N.Griffon, J.S.Henthorn, M.C.Marden, C.Poyart, I.Papassotiriou, D.Promé, F.Galactéros, S.C.Davies, and H.Wajcman (1997).
Alteration of an intersubunit contact in hemoglobin variants: comparative study of modifications at position alpha 126 Asp (H9).
  C R Acad Sci III, 320, 849-855.  
9032082 K.S.Kroeger, and C.E.Kundrot (1997).
Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.
  Structure, 5, 227-237.
PDB codes: 1abw 1aby
9223274 M.A.Schumacher, E.E.Zheleznova, K.S.Poundstone, R.Kluger, R.T.Jones, and R.G.Brennan (1997).
Allosteric intermediates indicate R2 is the liganded hemoglobin end state.
  Proc Natl Acad Sci U S A, 94, 7841-7844.
PDB codes: 1hab 1hac
  9361418 M.J.Weickert, M.Pagratis, S.R.Curry, and R.Blackmore (1997).
Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli.
  Appl Environ Microbiol, 63, 4313-4320.  
9216253 V.T.Ivanov, A.A.Karelin, M.M.Philippova, I.V.Nazimov, and V.Z.Pletnev (1997).
Hemoglobin as a source of endogenous bioactive peptides: the concept of tissue-specific peptide pool.
  Biopolymers, 43, 171-188.  
8647854 B.Vallone, A.Bellelli, A.E.Miele, M.Brunori, and G.Fermi (1996).
Probing the alpha 1 beta 2 interface of human hemoglobin by mutagenesis. Role of the FG-C contact regions.
  J Biol Chem, 271, 12472-12480.
PDB code: 1gli
8639491 E.Bucci, A.Razynska, H.Kwansa, Z.Gryczynski, J.H.Collins, C.Fronticelli, R.Unger, M.Braxenthaler, J.Moult, X.Ji, and G.Gilliland (1996).
Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin.
  Biochemistry, 35, 3418-3425.
PDB code: 1cls
8639610 H.W.Kim, T.J.Shen, N.T.Ho, M.Zou, M.F.Tam, and C.Ho (1996).
Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin.
  Biochemistry, 35, 6620-6627.  
8756522 I.A.Vakser (1996).
Low-resolution docking: prediction of complexes for underdetermined structures.
  Biopolymers, 39, 455-464.  
8639677 I.Pechik, X.Ji, K.Fidelis, M.Karavitis, J.Moult, W.S.Brinigar, C.Fronticelli, and G.L.Gilliland (1996).
Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.
  Biochemistry, 35, 1935-1945.
PDB codes: 1hdb 2hhd
8824225 N.Griffon, C.Badens, D.Lena-Russo, J.Kister, J.Bardakdjian, H.Wajcman, M.C.Marden, and C.Poyart (1996).
Hb Bruxelles, deletion of Phebeta42, shows a low oxygen affinity and low cooperativity of ligand binding.
  J Biol Chem, 271, 25916-25920.  
8602627 P.Lacan, J.Kister, A.Francina, G.Souillet, F.Galactéros, J.Delaunay, and H.Wajcman (1996).
Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable hemoglobin with twofold increased oxygen affinity.
  Am J Hematol, 51, 276-281.  
8968957 T.Ikehara, Y.Eguchi, S.Kayo, and H.Takei (1996).
Amino acid sequences of hemoglobin beta chains of five species of pinnipeds: Neophoca cinerea, Otaria byronia, Eumetopias jubatus, Pusa hispida, and Pagophilus groenlandica.
  J Protein Chem, 15, 659-665.  
  7555018 B.Giardina, I.Messana, R.Scatena, and M.Castagnola (1995).
The multiple functions of hemoglobin.
  Crit Rev Biochem Mol Biol, 30, 165-196.  
  8590629 G.A.Singer, T.Kleinschmidt, and G.Braunitzer (1995).
The primary structure of the hemoglobin from the lobe-lipped bat (Chalinolobus morio, Microchiroptera).
  Biol Chem Hoppe Seyler, 376, 603-609.  
8555060 G.Vassilopoulos, I.Papassotiriou, E.Voskaridou, A.Stamoulakatou, E.Premetis, J.Kister, M.Marden, N.Griffon, C.Poyart, and H.Wajcman (1995).
Hb Arta [beta 45 (CD4) Phe-->Cys]: a new unstable haemoglobin with reduced oxygen affinity in trans with beta-thalassaemia.
  Br J Haematol, 91, 595-601.  
7696517 J.Antosiewicz, and D.Porschke (1995).
Electrostatics of hemoglobins from measurements of the electric dichroism and computer simulations.
  Biophys J, 68, 655-664.  
  7773181 M.B.Swindells (1995).
A procedure for the automatic determination of hydrophobic cores in protein structures.
  Protein Sci, 4, 93.  
7829496 M.Nagai, S.Kaminaka, Y.Ohba, Y.Nagai, Y.Mizutani, and T.Kitagawa (1995).
Ultraviolet resonance Raman studies of quaternary structure of hemoglobin using a tryptophan beta 37 mutant.
  J Biol Chem, 270, 1636-1642.  
7592833 R.A.Hernan, and S.G.Sligar (1995).
Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.
  J Biol Chem, 270, 26257-26264.  
  8563637 R.M.Stroud, and E.B.Fauman (1995).
Significance of structural changes in proteins: expected errors in refined protein structures.
  Protein Sci, 4, 2392-2404.  
  8557026 U.Ermler, R.A.Siddiqui, R.Cramm, and B.Friedrich (1995).
Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 A resolution.
  EMBO J, 14, 6067-6077.
PDB code: 1cqx
8539249 W.L.Nichols, G.D.Rose, L.F.Ten Eyck, and B.H.Zimm (1995).
Rigid domains in proteins: an algorithmic approach to their identification.
  Proteins, 23, 38-48.  
7873588 Y.Arata (1995).
Effect of the tertiary structure alteration by ligation on the interface contacts between subunits of hemoglobin.
  Biochim Biophys Acta, 1247, 24-34.  
  7756993 A.A.Adzhubei, and M.J.Sternberg (1994).
Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building.
  Protein Sci, 3, 2395-2410.  
  7849579 D.Eisenberg, and M.Perutz (1994).
Max Perutz's achievements: how did he do it?
  Protein Sci, 3, 1625-1628.  
8202470 F.R.Smith, and K.C.Simmons (1994).
Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary structure.
  Proteins, 18, 295-300.  
  7849587 H.E.Aronson, W.E.Royer, and W.A.Hendrickson (1994).
Quantification of tertiary structural conservation despite primary sequence drift in the globin fold.
  Protein Sci, 3, 1706-1711.  
7972099 H.W.Kim, T.J.Shen, D.P.Sun, N.T.Ho, M.Madrid, M.F.Tam, M.Zou, P.F.Cottam, and C.Ho (1994).
Restoring allosterism with compensatory mutations in hemoglobin.
  Proc Natl Acad Sci U S A, 91, 11547-11551.  
7731951 I.A.Vakser, and C.Aflalo (1994).
Hydrophobic docking: a proposed enhancement to molecular recognition techniques.
  Proteins, 20, 320-329.  
  7756991 M.A.Rodionov, and M.S.Johnson (1994).
Residue-residue contact substitution probabilities derived from aligned three-dimensional structures and the identification of common folds.
  Protein Sci, 3, 2366-2377.  
  7994365 R.Kluger, R.T.Jones, and D.T.Shih (1994).
Cross-linking hemoglobin by design: lessons from using molecular clamps.
  Artif Cells Blood Substit Immobil Biotechnol, 22, 415-428.  
7972019 R.Srinivasan, and G.D.Rose (1994).
The T-to-R transformation in hemoglobin: a reevaluation.
  Proc Natl Acad Sci U S A, 91, 11113-11117.  
  7849602 S.E.Brenner, and A.Berry (1994).
A quantitative methodology for the de novo design of proteins.
  Protein Sci, 3, 1871-1882.  
8471730 A.Ansari, C.M.Jones, E.R.Henry, J.Hofrichter, and W.A.Eaton (1993).
Photoselection in polarized photolysis experiments on heme proteins.
  Biophys J, 64, 852-868.  
8274641 H.Gilch, R.Schweitzer-Stenner, and W.Dreybrodt (1993).
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.
  Biophys J, 65, 1470-1485.  
8451234 J.Janin, and S.J.Wodak (1993).
The quaternary structure of carbonmonoxy hemoglobin ypsilanti.
  Proteins, 15, 1-4.  
8513788 L.Martineau, and C.T.Craescu (1993).
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.
  Eur J Biochem, 214, 383-393.  
8251060 M.Oshima, S.Nakamura, and M.Z.Atassi (1993).
Amino acid substitutions outside a preselected antigenic region in hemoglobin affect the binding to monoclonal antibodies obtained by immunization with the synthetic region.
  J Protein Chem, 12, 403-412.  
8343575 M.Prabhakaran, and M.E.Johnson (1993).
Molecular dynamics of sickle and normal hemoglobins.
  Biopolymers, 33, 735-742.  
19431886 R.Schweitzer-Stenner, M.Bosenbeck, and W.Dreybrodt (1993).
Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect.
  Biophys J, 64, 1194-1209.  
  8401217 V.Baudin, J.Pagnier, L.Kiger, J.Kister, O.Schaad, M.T.Bihoreau, N.Lacaze, M.C.Marden, S.J.Edelstein, and C.Poyart (1993).
Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers.
  Protein Sci, 2, 1320-1330.  
8248322 Z.Gryczynski, E.Bucci, and J.Kuśba (1993).
Linear dichroism study of metalloporphyrin transition moments in view of radiationless interactions with tryptophan in hemoproteins.
  Photochem Photobiol, 58, 492-498.  
1324020 A.Levy, V.S.Sharma, L.Zhang, and J.M.Rifkind (1992).
A new mode for heme-heme interactions in hemoglobin associated with distal perturbations.
  Biophys J, 61, 750-755.  
1515540 D.L.Weaver (1992).
Hydrophobic interaction between globin helices.
  Biopolymers, 32, 477-490.  
1518802 D.L.Weaver (1992).
Modeling microdomains: the surface area of globin helices.
  Proteins, 13, 327-335.  
1549581 E.Katchalski-Katzir, I.Shariv, M.Eisenstein, A.A.Friesem, C.Aflalo, and I.A.Vakser (1992).
Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques.
  Proc Natl Acad Sci U S A, 89, 2195-2199.  
1603814 M.J.Sippl, and S.Weitckus (1992).
Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations.
  Proteins, 13, 258-271.  
1420905 Z.Gryczynski, T.Tenenholz, and E.Bucci (1992).
Rates of energy transfer between tryptophans and hemes in hemoglobin, assuming that the heme is a planar oscillator.
  Biophys J, 63, 648-653.  
2017435 A.P.Korn, and R.M.Burnett (1991).
Distribution and complementarity of hydropathy in multisubunit proteins.
  Proteins, 9, 37-55.  
2017436 C.Sander, and R.Schneider (1991).
Database of homology-derived protein structures and the structural meaning of sequence alignment.
  Proteins, 9, 56-68.  
2006159 F.C.Wireko, and D.J.Abraham (1991).
X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin.
  Proc Natl Acad Sci U S A, 88, 2209-2211.  
1896430 F.R.Smith, E.E.Lattman, and C.W.Carter (1991).
The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin.
  Proteins, 10, 81-91.
PDB code: 1cmy
1660134 G.Vriend, and C.Sander (1991).
Detection of common three-dimensional substructures in proteins.
  Proteins, 11, 52-58.  
  1678690 H.T.Wright (1991).
Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins.
  Crit Rev Biochem Mol Biol, 26, 1.  
1907667 J.Rose, and F.Eisenmenger (1991).
A fast unbiased comparison of protein structures by means of the Needleman-Wunsch algorithm.
  J Mol Evol, 32, 340-354.  
1896429 L.C.Andrews, and R.W.Harrison (1991).
Modeling conformational change in macromolecules as an elastic deformation.
  Proteins, 10, 162-170.  
2062828 M.E.Noble, R.K.Wierenga, A.M.Lambeir, F.R.Opperdoes, A.M.Thunnissen, K.H.Kalk, H.Groendijk, and W.G.Hol (1991).
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
  Proteins, 10, 50-69.
PDB codes: 1iig 1iih 6tim
2062827 R.K.Wierenga, M.E.Noble, J.P.Postma, H.Groendijk, K.H.Kalk, W.G.Hol, and F.R.Opperdoes (1991).
The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase.
  Proteins, 10, 33-49.
PDB code: 3tim
1862080 T.H.Jessen, R.E.Weber, G.Fermi, J.Tame, and G.Braunitzer (1991).
Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering.
  Proc Natl Acad Sci U S A, 88, 6519-6522.  
2235993 A.Pastore, and A.M.Lesk (1990).
Comparison of the structures of globins and phycocyanins: evidence for evolutionary relationship.
  Proteins, 8, 133-155.  
2385590 K.H.Ruan, J.Spurlino, F.A.Quiocho, and M.Z.Atassi (1990).
Acetylcholine receptor-alpha-bungarotoxin interactions: determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity.
  Proc Natl Acad Sci U S A, 87, 6156-6160.  
2107323 M.S.Johnson, M.J.Sutcliffe, and T.L.Blundell (1990).
Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.
  J Mol Evol, 30, 43-59.  
2622903 M.E.Karpen, Haseth, and K.E.Neet (1989).
Comparing short protein substructures by a method based on backbone torsion angles.
  Proteins, 6, 155-167.  
2775840 N.Ramasubbu, and R.Parthasarathy (1989).
Role of water molecules in the crystal structure of Gly-L-Ala-L-Phe: a possible sequence preference for nucleation of alpha-helix?
  Biopolymers, 28, 1259-1269.  
  2713096 T.Kleinschmidt, G.Braunitzer, and H.G.Scheil (1989).
Carnivora: the primary structure of the giant otter (Pteronura brasiliensis, Mustelidae) hemoglobin.
  Biol Chem Hoppe Seyler, 370, 35-40.  
  3348887 J.G.Sgouros, T.Kleinschmidt, and G.Braunitzer (1988).
The primary structure of the hemoglobin of the Indian false vampire (Megaderma lyra, Microchiroptera).
  Biol Chem Hoppe Seyler, 369, 47-53.  
3422453 S.A.Hefta, S.B.Lyle, M.R.Busch, D.E.Harris, J.B.Matthew, and F.R.Gurd (1988).
Site-specific semisynthetic variant of human hemoglobin.
  Proc Natl Acad Sci U S A, 85, 709-713.  
3447171 D.J.Abraham, and A.J.Leo (1987).
Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients.
  Proteins, 2, 130-152.  
3476938 G.Fermi, M.F.Perutz, and R.G.Shulman (1987).
Iron distances in hemoglobin: comparison of x-ray crystallographic and extended x-ray absorption fine structure studies.
  Proc Natl Acad Sci U S A, 84, 6167-6168.  
3463997 A.Bianconi, A.Congiu-Castellano, M.Dell'Ariccia, A.Giovannelli, S.Morante, E.Burattini, and P.J.Durham (1986).
Local Fe site structure in the tense-to-relaxed transition in carp deoxyhemoglobin: a XANES (x-ray absorption near edge structure) study.
  Proc Natl Acad Sci U S A, 83, 7736-7740.  
  3709526 C.Chothia, and A.M.Lesk (1986).
The relation between the divergence of sequence and structure in proteins.
  EMBO J, 5, 823-826.  
3956482 J.D.Smit, H.Sick, A.Peterhans, and K.Gersonde (1986).
Acid Bohr effect of a monomeric haemoglobin from Dicrocoelium dendriticum. Mechanism of the allosteric conformation transition.
  Eur J Biochem, 155, 231-237.  
3856881 E.R.Henry, M.Levitt, and W.A.Eaton (1985).
Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin.
  Proc Natl Acad Sci U S A, 82, 2034-2038.  
3860865 F.R.Smith, and G.K.Ackers (1985).
Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin.
  Proc Natl Acad Sci U S A, 82, 5347-5351.  
3903751 K.Nagai, M.F.Perutz, and C.Poyart (1985).
Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.
  Proc Natl Acad Sci U S A, 82, 7252-7255.  
6589624 M.F.Perutz, G.Fermi, and T.B.Shih (1984).
Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.
  Proc Natl Acad Sci U S A, 81, 4781-4784.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.