Document Detail

Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin.
MedLine Citation:
PMID:  23283700     Owner:  NLM     Status:  Publisher    
The hydrophobic effect is associated with the successive replacement of water molecules in the binding site of a protein by hydrophobic groups of the ligand. Although the hydrophobic effect is assumed to be entropy-driven, large changes in enthalpy and entropy are observed with the model system thermolysin. Structural changes in the binding features of the water molecules ultimately determine the thermodynamics of the hydrophobic effect.
Adam Biela; Nader N Nasief; Michael Betz; Andreas Heine; David Hangauer; Gerhard Klebe
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-2
Journal Detail:
Title:  Angewandte Chemie (International ed. in English)     Volume:  -     ISSN:  1521-3773     ISO Abbreviation:  Angew. Chem. Int. Ed. Engl.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370543     Medline TA:  Angew Chem Int Ed Engl     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Department of Pharmaceutical Chemistry, Philipps-University Marburg, Marbacher Weg 6, 35032 Marburg (Germany).
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