Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme.

Abstract:

:Activation enthalpies and entropies are reported for proton-deuteron exchange at 42 amide sites in T4 lysozyme and compared with activation volumes for the same residues obtained earlier [Hitchens, T. K., and Bryant, R. G. (1998) Biochemistry 37, 5878-5887]. There is no correlation found between activation volume and activation entropy or activation enthalpy. The activation enthalpy is linearly related to the activation entropy in part as a consequence of a relatively narrow sampling window for the rate constants that corresponds to a narrow range of activation free energy. A consequence of the entropy-enthalpy compensation is preservation of rank order of proton exchange. Variations in DeltaH, DeltaS, and DeltaV for residues that are structurally close together in the folded protein suggest that there may be a variety of energetically distinct pathways for the access of solvent to these structurally related exchange sites.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Dixon ME,Hitchens TK,Bryant RG

doi

10.1021/bi991718y

subject

Has Abstract

pub_date

2000-01-11 00:00:00

pages

248-54

issue

1

eissn

0006-2960

issn

1520-4995

pii

bi991718y

journal_volume

39

pub_type

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