Literature DB >> 1609279

Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin.

S W Englander1, J J Englander, R E McKinnie, G K Ackers, G J Turner, J A Westrick, S J Gill.   

Abstract

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.

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Year:  1992        PMID： 1609279      PMCID： PMC3562468          DOI： 10.1126/science.256.5064.1684

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  26 in total

1.  Protein hydrogen exchange studied by the fragment separation method.

Authors:  J J Englander; J R Rogero; S W Englander
Journal:  Anal Biochem       Date:  1985-05-15       Impact factor: 3.365

2.  Individual breathing reactions measured by functional labeling and hydrogen exchange methods.

Authors:  J R Rogero; J J Englander; S W Englander
Journal:  Methods Enzymol       Date:  1986       Impact factor: 1.600

Review 3.  Hydrogen exchange in proteins.

Authors:  A Hvidt; S O Nielsen
Journal:  Adv Protein Chem       Date:  1966

4.  Stereochemistry of cooperative effects in haemoglobin.

Authors:  M F Perutz
Journal:  Nature       Date:  1970-11-21       Impact factor: 49.962

5.  Allosteric sensitivity in hemoglobin at the alpha-subunit N-terminus studied by hydrogen exchange.

Authors:  J Ray; S W Englander
Journal:  Biochemistry       Date:  1986-05-20       Impact factor: 3.162

6.  Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins.

Authors:  S H Ip; G K Ackers
Journal:  J Biol Chem       Date:  1977-01-10       Impact factor: 5.157

7.  Identification of an allosterically sensitive unfolding unit in hemoglobin.

Authors:  J J Englander; J R Rogero; S W Englander
Journal:  J Mol Biol       Date:  1983-09-05       Impact factor: 5.469

8.  Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state.

Authors:  F C Mills; G K Ackers
Journal:  J Biol Chem       Date:  1979-04-25       Impact factor: 5.157

9.  Oxygen binding constants for human hemoglobin tetramers.

Authors:  S J Gill; E Di Cera; M L Doyle; G A Bishop; C H Robert
Journal:  Biochemistry       Date:  1987-06-30       Impact factor: 3.162

10.  Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchange.

Authors:  G Louie; J J Englander; S W Englander
Journal:  J Mol Biol       Date:  1988-06-20       Impact factor: 5.469
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  22 in total

1.  On the roles of substrate binding and hinge unfolding in conformational changes of adenylate kinase.

Authors:  Jason B Brokaw; Jhih-Wei Chu
Journal:  Biophys J       Date:  2010-11-17       Impact factor: 4.033

2.  Cooperative alpha-helix unfolding in a protein-DNA complex from hydrogen-deuterium exchange.

Authors:  Roberto K Salinas; Tammo Diercks; Robert Kaptein; Rolf Boelens
Journal:  Protein Sci       Date:  2006-06-02       Impact factor: 6.725

3.  Probing high order structure of proteins by fast-atom bombardment mass spectrometry.

Authors:  Y Liu; D L Smith
Journal:  J Am Soc Mass Spectrom       Date:  1994-01       Impact factor: 3.109

Review 4.  Mechanisms and uses of hydrogen exchange.

Authors:  S W Englander; T R Sosnick; J J Englander; L Mayne
Journal:  Curr Opin Struct Biol       Date:  1996-02       Impact factor: 6.809

5.  The orientation and dynamics of substance P in lipid environments.

Authors:  D A Keire; M Kobayashi
Journal:  Protein Sci       Date:  1998-11       Impact factor: 6.725

6.  Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR.

Authors:  B E Jones; C R Matthews
Journal:  Protein Sci       Date:  1995-02       Impact factor: 6.725

7.  Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry.

Authors:  Z Zhang; D L Smith
Journal:  Protein Sci       Date:  1996-07       Impact factor: 6.725

8.  Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation.

Authors:  Z Zhang; D L Smith
Journal:  Protein Sci       Date:  1993-04       Impact factor: 6.725

9.  Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry.

Authors:  Joan J Englander; Charyl Del Mar; Will Li; S Walter Englander; Jack S Kim; David D Stranz; Yoshitomo Hamuro; Virgil L Woods
Journal:  Proc Natl Acad Sci U S A       Date:  2003-05-28       Impact factor: 11.205

10.  On the pH dependence of amide proton exchange rates in proteins.

Authors:  M A Eriksson; T Härd; L Nilsson
Journal:  Biophys J       Date:  1995-08       Impact factor: 4.033
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