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PMID: 1710937 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1.

Biophysical journal ·Vol. 59 ·No. 3 ·1991-03-00 ·Pages 516-22

Rath P, Bousché O, Merrill AR, Cramer WA, Rothschild KJ

Abstract

The structure of the membrane bound state of the 178-residue thermolytic COOH-terminal channel forming peptide of colicin E1 was studied by polarized Fourier transform infrared (FTIR) spectroscopy. This fragment was reconstituted into DMPC liposomes at varying peptide/lipid ratios ranging from 1/25-1/500. The amide I band frequency of the protein indicated a dominant alpha-helical secondary structure with limited beta- and random structures. The amide I and II frequencies are at 1,656 and 1,546 cm-1, close to the frequency of the amide I and II bands of rhodopsin, bacteriorhodopsin and other alpha-helical proteins. Polarized FTIR of oriented membranes revealed that the alpha-helices have an average orientation less than the magic angle, 54.6 degrees, relative to the membrane normal. Almost all of the peptide groups in the membrane-bound channel protein undergo rapid hydrogen/deuterium (H/D) exchange. These results are contrasted to the alpha-helical membrane proteins, bacteriorhodopsin, and rhodopsin.

MeSH Terms
Biophysical Phenomena Biophysics Cell Membrane/chemistry Colicins/chemistry,pharmacology Escherichia coli/analysis,drug effects Fourier Analysis Ion Channels/chemistry,drug effects Molecular Structure Protein Conformation Solubility Spectrophotometry, Infrared Water
Chemicals
Colicins Ion Channels Water
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Rath P
Physics Department, Boston University, Massachusetts 02215.
Bousché O
Merrill A R
Cramer W A
Rothschild K J
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37 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(91)82268-8
Published
1991-03-00
Pages
516-22
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1281217
Subset
IM
Grants
NEI NIH HHS · EY05499 · United States
NIGMS NIH HHS · GM18457 · United States
External Links
PubMed source DOI: 10.1016/S0006-3495(91)82268-8 PMC Full Text View journal details
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