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Proceedings of the National Academy of Sciences of the United States of America

Volumn 99, Issue 15, 2002, Pages 9777-9782

Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function

(5) Ackers, Gary K a Dalessio, Paula M b Lew, George H c Daugherty, Margaret A d Holt, Jo M a

a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE (United States)

b PENN STATE COLLEGE OF MEDICINE (United States)

c LOYOLA UNIVERSITY MEDICAL CENTER (United States)

d UNIVERSITY OF VERMONT (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; HEMOGLOBIN; TETRAMER;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; COVALENT BOND; HYDROGEN BOND; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; RESIDUE ANALYSIS; THERMODYNAMICS;

BINDING SITES; DIMERIZATION; HEMOGLOBIN A; HEMOGLOBINS; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN HYBRIDIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 0037162515 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.152225999 Document Type: Article

Times cited : (32)

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