Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-1-28
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-54
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme.
pubmed:affiliation
Department of Chemistry, University of Virginia, Charlottesville 22901, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't