Document Detail


Adsorption of proteins on a lipid bilayer.
MedLine Citation:
PMID:  20386900     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In our analysis of protein adsorption on a lipid bilayer, the protein surface is considered to contain one or a few charged spots, and the bilayer contains a significant amount of lipids with oppositely charged head groups. After adsorption, a folded protein is assumed to change its shape slightly due to the electrostatic attraction, so that one of the spots forms a flat contact with the oppositely charged lipid heads of the lipid bilayer. With realistic parameters, this model predicts that the contribution of electrostatic interactions to the protein adsorption energy per charged amino acid-lipid pair is 16-25 kJ/mol. Thus, a few (four or five) pairs is sufficient for irreversible adsorption.
Authors:
Vladimir P Zhdanov; Bengt Kasemo
Publication Detail:
Type:  Journal Article     Date:  2010-04-13
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  39     ISSN:  1432-1017     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-09-22     Completed Date:  2011-01-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  1477-82     Citation Subset:  IM    
Affiliation:
Department of Applied Physics, Chalmers University of Technology, 412 96 Göteborg, Sweden. zhdanov@catalysis.ru
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MeSH Terms
Descriptor/Qualifier:
Adsorption
Lipid Bilayers / chemistry*,  metabolism
Protein Folding
Proteins / chemistry*,  metabolism
Static Electricity
Thermodynamics
Chemical
Reg. No./Substance:
0/Lipid Bilayers; 0/Proteins

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


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