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Science 19 June 1992:
Vol. 256. no. 5064, pp. 1684 - 1687
DOI: 10.1126/science.256.5064.1684
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Articles

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

S. Walter Englander , Joan J. Englander , Russell E. McKinnie , Gary K. Ackers , George J. Turner , Judy A. Westrick , and Stanley J. Gill

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mass Spectrometric Approaches Using Electrospray Ionization Charge States and Hydrogen-Deuterium Exchange for Determining Protein Structures and Their Conformational Changes.
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Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.
J. J. Englander, C. Del Mar, W. Li, S. W. Englander, J. S. Kim, D. D. Stranz, Y. Hamuro, and V. L. Woods Jr. (2003)
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Hydrogen Exchange-Mass Spectrometry: Optimization of Digestion Conditions.
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Backbone Dynamics of Plastocyanin in Both Oxidation States. SOLUTION STRUCTURE OF THE REDUCED FORM AND COMPARISON WITH THE OXIDIZED STATE.
I. Bertini, D. A. Bryant, S. Ciurli, A. Dikiy, C. O. Fernandez, C. Luchinat, N. Safarov, A. J. Vila, and J. Zhao (2001)
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Protein folding intermediates: native-state hydrogen exchange.
Y Bai, T. Sosnick, L Mayne, and S. Englander (1995)
Science 269, 192-197
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Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A.
S. Mayo and R. Baldwin (1993)
Science 262, 873-876
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Structural Characterization of Protein Kinase A as a Function of Nucleotide Binding. HYDROGEN-DEUTERIUM EXCHANGE STUDIES USING MATRIX-ASSISTED LASER DESORPTION IONIZATION-TIME OF FLIGHT MASS SPECTROMETRY DETECTION.
M. D. Andersen, J. Shaffer, P. A. Jennings, and J. A. Adams (2001)
J. Biol. Chem. 276, 14204-14211
   Abstract »    Full Text »    PDF »
A signature of the T right-arrow R transition in human hemoglobin.
M.-R. Mihailescu and I. M. Russu (2001)
PNAS 98, 3773-3777
   Abstract »    Full Text »    PDF »


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