Document Detail

Mathematical modelling of electrostatic fluctuations in subtilisin active site.
MedLine Citation:
PMID:  7779299     Owner:  NLM     Status:  MEDLINE    
The intensities of electrostatic fluctuations in subtilisin active site generated by conformational motion of charged side chains, polar side chains and peptide bonds of the main chain are calculated. The comparative analysis of all these fragments reveals that there are few of them which make the main contribution to the total value of the intensity, which has been found to be approximately 10(7) These are Ser 125, Thr 220 and peptide bonds of aminoacids 125-126, 218-219. Our present analysis enables us to compare the relative contribution of different fragments but we do not pretend to obtain precise absolute values. The reason for this is the lack of the detailed selective information on the mean-square amplitudes and correlation times of conformational motion of the fragments and on the values of local dielectric constants in the interior of subtilisin. The possibility for electrostatic fluctuations in enzyme active site to be an efficient nonspecific source of substrate activation is discussed.
L V Lopoukhov; A E Sitnitsky; V D Fedotov
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biomolecular structure & dynamics     Volume:  12     ISSN:  0739-1102     ISO Abbreviation:  J. Biomol. Struct. Dyn.     Publication Date:  1995 Feb 
Date Detail:
Created Date:  1995-07-17     Completed Date:  1995-07-17     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8404176     Medline TA:  J Biomol Struct Dyn     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  767-84     Citation Subset:  IM    
Laboratory of Molecular Biophysics, Institute of Biology, Kazan, Tatarstan, Russia.
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MeSH Terms
Binding Sites
Computer Simulation*
Models, Chemical*
Protein Conformation
Subtilisins / chemistry*
Reg. No./Substance:
EC 3.4.21.-/Subtilisins

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