Document Detail


Altering the orientation of proteins on self-assembled monolayers: a computational study.
MedLine Citation:
PMID:  18847238     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A combined computational docking-molecular dynamics study has been performed on a system consisting of cytochrome c protein and alkanethiol self-assembled monolayers of various geometries. The results suggest that the orientation of the protein on the surface may be controlled or altered by means of designing specific structural motifs on the surface. The proposed computational approach may be used as a fast and reliable tool to complement other theoretical and experimental techniques of exploring other protein-surface interfaces.
Authors:
Bartosz Trzaskowski; Filip Leonarski; Andrzej Leś; Ludwik Adamowicz
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-10-11
Journal Detail:
Title:  Biomacromolecules     Volume:  9     ISSN:  1526-4602     ISO Abbreviation:  Biomacromolecules     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-11-10     Completed Date:  2008-12-24     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100892849     Medline TA:  Biomacromolecules     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3239-45     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University of Arizona, Tucson, Arizona 85716, USA. trzask@wag.caltech.edu
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MeSH Terms
Descriptor/Qualifier:
Adsorption*
Computer Simulation
Cytochromes c / chemistry
Models, Theoretical*
Protein Binding
Proteins / chemistry*
Sulfhydryl Compounds / chemistry
Chemical
Reg. No./Substance:
0/Proteins; 0/Sulfhydryl Compounds; 9007-43-6/Cytochromes c

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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