Role of subunit interfaces in the allosteric mechanism of hemoglobin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 11 ·1976-11-00 ·Pages 3793-7

Chothia C, Wodak S, Janin J

Abstract

We calculate the surface area buried in subunit interfaces of human deoxyhemoglobin and of horse methemoglobin. A larger surface area is buried in deoxy- than in methemoglobin as a result of tertiary and quaternary structure changes. In both molecules the dimer-dimer interface is closepacked. This implies that hydrophobicity stabilizes the deoxystructure, the free energy spent in keeping the subunits in a low-affinity conformation being compensated by hydrophobic free energy due to the smaller surface area accessible to solvent.

MeSH Terms

Allosteric Regulation Animals Hemoglobin A Hemoglobins Horses Humans Methemoglobin Protein Conformation Structure-Activity Relationship Thermodynamics

Chemicals

Hemoglobins Methemoglobin Hemoglobin A

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Chothia C

Wodak S

Janin J

References (18)

18 references, click to expand

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Article Info

Journal

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

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.73.11.3793

Published

1976-11-00

Pages

3793-7

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC431212

Subset

External Links

PubMed source DOI: 10.1073/pnas.73.11.3793 PMC Full Text View journal details

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Role of subunit interfaces in the allosteric mechanism of hemoglobin.

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