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PMID: 6183433 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Ion interactions in (1-13C)D-Val8 and D-Leu14 analogs of gramicidin A, the helix sense of the channel and location of ion binding sites.

The Journal of membrane biology ·Vol. 69 ·No. 3 ·1982-00-00 ·Pages 225-31

Urry DW, Walker JT, Trapane TL

Abstract

Ion-induced chemical shifts in the carbonyl carbon resonances of synthesized ad verified (1-13C)D-Val8 gramicidin A and (1-13C)D-Leu14 gramicidin A are utilized in combination with the previously determined location of the ion binding sites of the gramicidin A channel (using the carbonyls of L-residues) to determine that the helix sense of the gramicidin A channel) is left-handed. Having resolved the handedness issue, the location of the ion binding sites (which are fundamental to understanding the mechanism of ion transport) are further delineated with the results indicating two sites separated by just over 20 A. Furthermore, the demonstration that the divalent barium ion interacts at the binding site while not being transported through the channel is used to argue that the mechanism of monovalent vs. divalent cation selectivity is due to the positive image force contribution to the central barrier.

MeSH Terms
Biological Transport Carbon Isotopes Gramicidin/chemical synthesis Ion Channels/physiology Lipid Bilayers Models, Biological Protein Binding Protein Conformation Structure-Activity Relationship
Chemicals
Carbon Isotopes Ion Channels Lipid Bilayers Gramicidin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Urry D W
Walker J T
Trapane T L
References (31)
31 references, click to expand
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Article Info
Journal
The Journal of membrane biology
Abbr.
J Membr Biol
ISSN
0022-2631
DOI
10.1007/BF01870401
Published
1982-00-00
Pages
225-31
Language
English
Region
United States
NLM ID
0211301
Subset
IM
Grants
NIGMS NIH HHS · GM-26898 · United States
External Links
PubMed source DOI: 10.1007/BF01870401 View journal details
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