Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 10 ·1991-05-15 ·Pages 4472-5

Eaton WA, Henry ER, Hofrichter J

Abstract

The transition state for the R in equilibrium with T quaternary conformational change of hemoglobin has thermodynamic properties much closer to those of the R conformation than to those of the T conformation. This finding is based on a comparison of activation and equilibrium enthalpy and entropy changes and on the observation of a linear free energy relationship between quaternary rate and equilibrium constants. A previous theoretical study [Janin, J. & Wodak, S. J. (1985) Biopolymers 24, 509-526], using a highly simplified energy function, suggests that the R-like transition state is the result of a reaction pathway with the maximum buried surface area between alpha beta dimers.

MeSH Terms

Allosteric Regulation Hemoglobins/chemistry Humans Kinetics Macromolecular Substances Protein Conformation Thermodynamics

Chemicals

Hemoglobins Macromolecular Substances

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Eaton W A

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

Henry E R

Hofrichter J

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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.88.10.4472

Published

1991-05-15

Pages

4472-5

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC51682

Subset

External Links

PubMed source DOI: 10.1073/pnas.88.10.4472 PMC Full Text View journal details

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Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

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