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 related 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.
Englander
S W
SW
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059.
Englander
J J
JJ
McKinnie
R E
RE
Ackers
G K
GK
Turner
G J
GJ
Westrick
J A
JA
Gill
S J
SJ
D000494:Allosteric Regulation; D000495:Allosteric Site; D004735:Energy Transfer; D006454:Hemoglobins / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism*; D007474:Ion Exchange; D015394:Molecular Structure
D006454:Hemoglobins; D006859:Hydrogen