Publication Date:
1990-02-02
Description:
Protein unfolding and the dissolution of hydrophobic compounds (including solids, liquids, and gases) in water are characterized by a linear relation between entropy change and heat capacity change. The same slope is found for various classes of compounds, whereas the intercept depends on the particular class. The feature common to these processes is exposure of hydrophobic groups to water. These observations make possible the assignment of the heat capacity change to hydrophobic solvation and lead to the description of protein stability in terms of a hydrophobic and a nonhydrophobic contribution. A general representation of protein stability is given by the heat capacity change and the temperature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, K P -- Privalov, P L -- Gill, S J -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):559-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300815" target="_blank"〉PubMed〈/a〉
Keywords:
Chemical Phenomena
;
Chemistry
;
*Protein Denaturation
;
*Proteins
;
Thermodynamics
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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