Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-10-18
pubmed:abstractText
This paper describes a method for the evaluation of the unfolding heat capacity change of proteins by their amino-acid composition. The method hinges on a set of hydration heat capacity changes of amino acids extracted from the Protein Data Bank of crystallographic structures (Oobatake, M. and Ooi, T. (1988) J. Biochem. (Tokyo) 104, 433-439). This avoids problems linked to the choice of an arbitrary reference state. The published values have been normalized with respect to the total surface area of each amino-acid residue and related to the non-polar surface. The relationship found for amino acids allows a straightforward estimate of the unfolding heat capacity change of globular proteins. Predicted values for a large set of proteins fall within the experimental error. The devised algorithm shows that the unfolding heat capacity change depends on chain length and provides an explanation for the physical limits imposed upon this quantity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
1208
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-21
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Determination of hydrophobic hydration in protein unfolding by an intrinsic reference state.
pubmed:affiliation
Department of Biochemistry and Biophysics, 2nd University of Naples, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't