Document Detail

Determination of hydrophobic hydration in protein unfolding by an intrinsic reference state.
MedLine Citation:
PMID:  8086428     Owner:  NLM     Status:  MEDLINE    
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.
R Ragone; G Colonna
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1208     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1994 Sep 
Date Detail:
Created Date:  1994-10-18     Completed Date:  1994-10-18     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  15-21     Citation Subset:  IM    
Department of Biochemistry and Biophysics, 2nd University of Naples, Italy.
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MeSH Terms
Amino Acids / chemistry
Chemistry, Physical
Physicochemical Phenomena
Protein Folding*
Reg. No./Substance:
0/Amino Acids

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