Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin A

Smith R., Thomas D.E., Separovic F., Atkins A.R. and Cornell B.A. (1989) Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin A. Biophysical Journal, 56 2: 307-314.

Author Smith R.
Thomas D.E.
Separovic F.
Atkins A.R.
Cornell B.A.
Title Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin A
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
Publication date 1989-01-01
Sub-type Article (original research)
Open Access Status Not Open Access
Volume 56
Issue 2
Start page 307
End page 314
Total pages 8
Subject 1304 Biophysics
Abstract End-to-end helical dimers of gramicidin A form transmembrane pores in lipid bilayers, through which monovalent ions may pass. The groups within the peptide that interact with these ions have been studied by application of solid-state spectroscopic methods to a series of gramicidin A analogues synthesized with 13C in selected peptide carbonyl groups. The resonances of D-Leu10, D-Leu12 and D-Leu14 analogues were perturbed in the presence of 0.16 M sodium ions, whereas the resonances of the carbonyls of Gly2, Ala3, D-Leu4 and Val7, which are closer to the formylated N-terminal end of the peptide, were unaffected. The observed changes in chemical shift anisotropy are indicative of a change in orientation of the abovementioned leucine carbonyls.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
Versions
Version Filter Type
Citation counts: Scopus Citation Count Cited 58 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 28 Jun 2016, 17:37:53 EST by System User