Document Detail


Topography of the membrane-binding domain of cytochrome b5 in lipids by Fourier-transform infrared spectroscopy.
MedLine Citation:
PMID:  2176852     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Fourier-transform infrared spectroscopy was used to examine the secondary structure of the membrane-binding domain (nonpolar peptide) of rabbit liver cytochrome b5 in D2O and in the presence of phospholipids and deoxycholate. In all situations, the predominant structure was alpha helix, but an examination of the components of the amide I band in the spectrum of the nonpolar peptide showed that the major peak was shifted from 1655 cm-1 in the lipids to 1650 cm-1 in deoxycholate. This shift to lower frequency, together with a decrease in intensity of the amide II band, is indicative of N-H to N-D exchange of the peptide backbone. A semiquantitative analysis indicated that the alpha helix of the peptide is over 95% exchanged in the presence of deoxycholate but is only 10% exchanged in the presence of lipid. These data suggest that the membrane-inserted portion of the peptide is alpha helical and is largely protected from N-H to N-D exchange by the bilayer. We suggest that this technique appears to provide a general method for determining the type of secondary structure involved in membrane interaction and the percentage of this structure which is involved in the interaction.
Authors:
P W Holloway; C Buchheit
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  29     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1990 Oct 
Date Detail:
Created Date:  1991-02-25     Completed Date:  1991-02-25     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  9631-7     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Virginia School of Medicine, Charlottesville 22908.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Binding Sites
Circular Dichroism
Cytochromes b5 / chemistry,  metabolism*
Deoxycholic Acid / pharmacology*
Deuterium
Deuterium Oxide
Fourier Analysis
Liver / metabolism
Membranes / metabolism
Molecular Sequence Data
Phospholipids / pharmacology*
Protein Conformation
Rabbits
Spectrometry, Fluorescence
Spectrophotometry, Infrared / methods
Water
Grant Support
ID/Acronym/Agency:
GM 23858/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Phospholipids; 7732-18-5/Water; 7782-39-0/Deuterium; 7789-20-0/Deuterium Oxide; 83-44-3/Deoxycholic Acid; 9035-39-6/Cytochromes b5

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


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