Title
Conformational analysis, solvent-accessible surface and geometric extent of inhibitors and substrates Conformational analysis, solvent-accessible surface and geometric extent of inhibitors and substrates
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Publication type
article
Publication
Praha ,
Subject
Chemistry
Source (journal)
Collection of Czechoslovak chemical communications. - Praha
Volume/pages
71(2006) :6 , p. 842-858
ISSN
0010-0765
ISI
000238419500008
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Abstract
Peptide ligands are known to often bind in an extended conformation to maximize the contact surface with the receptor. The complementarity of shape and surface is a very important factor contributing to the stability of a ligand receptor complex. In this communication we try to answer the following questions: What is the influence of conformation on the surface area? Do ligands maximize their contact surface with the receptor to increase stability of the complex?
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