| Altering the orientation of proteins on self-assembled monolayers: a computational study. | |
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MedLine Citation:
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PMID: 18847238 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Bartosz Trzaskowski; Filip Leonarski; Andrzej Leś; Ludwik Adamowicz |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. Date: 2008-10-11 |
Journal Detail:
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Title: Biomacromolecules Volume: 9 ISSN: 1526-4602 ISO Abbreviation: Biomacromolecules Publication Date: 2008 Nov |
Date Detail:
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Created Date: 2008-11-10 Completed Date: 2008-12-24 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100892849 Medline TA: Biomacromolecules Country: United States |
Other Details:
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Languages: eng Pagination: 3239-45 Citation Subset: IM |
Affiliation:
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Department of Chemistry, University of Arizona, Tucson, Arizona 85716, USA. trzask@wag.caltech.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adsorption* Computer Simulation Cytochromes c / chemistry Models, Theoretical* Protein Binding Proteins / chemistry* Sulfhydryl Compounds / chemistry |
| Chemical | |
Reg. No./Substance:
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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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