Solid-state 13C-NMR studies of the effects of sodium ions on the gramicidin A ion channel

Smith, Ross, Thomas, Denise E., Atkins, Annette R., Separovic, Frances and Cornell, Bruce A. (1990) Solid-state 13C-NMR studies of the effects of sodium ions on the gramicidin A ion channel. BBA - Biomembranes, 1026 2: 161-166. doi:10.1016/0005-2736(90)90059-W


Author Smith, Ross
Thomas, Denise E.
Atkins, Annette R.
Separovic, Frances
Cornell, Bruce A.
Title Solid-state 13C-NMR studies of the effects of sodium ions on the gramicidin A ion channel
Journal name BBA - Biomembranes   Check publisher's open access policy
ISSN 0005-2736
Publication date 1990-07-24
Sub-type Article (original research)
DOI 10.1016/0005-2736(90)90059-W
Open Access Status Not yet assessed
Volume 1026
Issue 2
Start page 161
End page 166
Total pages 6
Language eng
Subject 1304 Biophysics
1303 Biochemistry
1307 Cell Biology
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 C in selected peptide carbonyl groups. The resonances of d-Leu, d-Leu and d-Leu analogues were perturbed in the presence of 0.16 M sodium ions, whereas the resonances of the carbonyls of Gly, Ala, d-Leu and Val, 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.
Keyword C-
Gramicidin A
Ion binding
Lipid bilayer
NMR
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
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Created: Fri, 15 Dec 2017, 03:51:42 EST