Document Detail

Structural investigation of the covalent and electrostatic binding of yeast cytochrome c to the surface of various ultrathin lipid multilayers using x-ray diffraction.
MedLine Citation:
PMID:  1648415     Owner:  NLM     Status:  MEDLINE    
X-Ray diffraction was used to characterize the profile structures of ultrathin lipid multilayers having a bound surface layer of cytochrome c. The lipid multilayers were formed on an alkylated glass surface, using the Langmuir-Blodgett method. The ultrathin lipid multilayers of this study were: five monolayers of arachidic acid, four monolayers of arachidic acid with a surface monolayer of dimyristoyl phosphatidylserine, and four monolayers of arachidic acid acid with a surface monolayer of thioethyl stearate. Both the phosphatidylserine and the thioethyl stearate surfaces were found previously to covalently bind yeast cytochrome c, while the arachidic acid surface electrostatically binds yeast cytochrome c. Meridional x-ray diffraction data were collected from these lipid multilayer films with and without a bound yeast cytochrome c surface layer. A box refinement technique, previously shown to be effective in deriving the profile structures of ultrathin multilayer lipid films with and without electrostatically bound cytochrome c, was used to determine the multilayer electron density profiles. The surface monolayer of bound cytochrome c was readily apparent upon comparison of the multilayer electron density profiles for the various pairs of ultrathin multilayer films plus/minus cytochrome c for all cases. In addition, cytochrome c binding to the multilayer surface significantly perturbs the underlying lipid monolayers.
J M Pachence; J K Blasie
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biophysical journal     Volume:  59     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  1991 Apr 
Date Detail:
Created Date:  1991-08-14     Completed Date:  1991-08-14     Revised Date:  2010-09-07    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  894-900     Citation Subset:  IM    
Chemistry Department, University of Pennsylvania, Philadelphia 19104.
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MeSH Terms
Cytochrome c Group / chemistry,  metabolism*
Molecular Conformation
Protein Binding
Saccharomyces cerevisiae / metabolism
X-Ray Diffraction
Reg. No./Substance:
0/Cytochrome c Group; 0/Liposomes

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