Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: Binding of phosphonamidate to the S1'-pocket of thermolysin

Prerequisite for the design of tight binding protein inhibitors and prediction of their properties is an in-depth understanding of the structural and thermodynamic details of the binding process. A series of closely related phosphonamidates was studied to elucidate the forces underlying their bindin...

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Bibliographic Details

Published in:	Biochimica et biophysica acta Vol. 1800; no. 11; pp. 1192 - 1202
Main Authors:	Englert, L., Biela, A., Zayed, M., Heine, A., Hangauer, D., Klebe, G.
Format:	Journal Article
Language:	English
Published:	Netherlands 01.11.2010
Subjects:	Binding Sites Crystallography, X-Ray Entropy Hydrophobic and Hydrophilic Interactions Models, Molecular Organophosphorus Compounds - chemistry Organophosphorus Compounds - metabolism Phosphoamino Acids - chemistry Protein Binding Protein Structure, Tertiary Thermodynamics Thermolysin - metabolism Water - chemistry Water - metabolism
ISSN:	0304-4165, 0006-3002
Online Access:	Get full text
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