Hydrogen Exchange Measurement of the Free Energy of Structural and Allosteric Change in Hemoglobin

The inability to localize and measure the free energy of protein structure and structure change severely limits protein structure-function investigations. The local unfolding model for protein hydrogen exchange quantitatively relates the free energy of local structural stability with the hydrogen ex...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1992-06, Vol.256 (5064), p.1684-1687
Main Authors: Englander, S. Walter, Englander, Joan J., McKinnie, Russell E., Ackers, Gary K., Turner, George J., Westrick, Judy A., Gill, Stanley J.
Format: Article
Language:English
Subjects:
allosteric properties
Allosteric proteins
Allosteric Regulation
Allosteric Site
Analytical, structural and metabolic biochemistry
Biochemistry
Biological and medical sciences
Conformation
Dimers
energy
Energy Transfer
exchange
Free energy
Fundamental and applied biological sciences. Psychology
haemoglobin
Hemoglobin
Hemoglobins
Hemoglobins - metabolism
Hemoproteins
Hydrogen
Hydrogen - metabolism
Hydrogen bonds
Ion Exchange
Legends
Metalloproteins
Molecular Structure
Phosphates
Protein conformation
Proteins
protons
Structural stability
structure
Tritium
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Summary:The inability to localize and measure the free energy of protein structure and structure change severely limits protein structure-function investigations. The local unfolding model for protein hydrogen exchange quantitatively relates the free energy of local structural stability with the hydrogen exchange rate of concerted sets of structurally related protons. In tests with a number of modified hemoglobin forms, the loss in structural free energy obtained locally from hydrogen exchange results matches the loss in allosteric free energy measured globally by oxygen-binding and subunit dissociation experiments.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.256.5064.1684