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Science 9 September 1983:
Vol. 221. no. 4615, pp. 1064 - 1067
DOI: 10.1126/science.221.4615.1064
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Articles

Is the Gramicidin A Transmembrane Channel Single-Stranded or Double-Stranded Helix? A Simple Unequivocal Determination

DAN W. URRY 1, TINA L. TRAPANE 1, and KARI U. PRASAD 1

1 Laboratory of Molecular Biophysics, University of Alabama School of Medicine, Birmingham 35294

Thallium ion-induced carbonyl carbon chemical shifts were compared for all of the L-residue-peptide carbonyl carbons of the gramicidin A transmembrane channel. Molecular structures were deduced by using the argument that helically equivalent and equally proximal carbonyls would exhibit essentially equivalent ion-induced chemical shifts. The transmembrane channel was found to be a head-to-head dimer with the structure of a left-handed, single-stranded beta-helix.

Submitted on March 22, 1983


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Transmembrane channels based on tartaric acid-gramicidin A hybrids.
C. Stankovic, S. Heinemann, J. Delfino, F. Sigworth, and S. Schreiber (1989)
Science 244, 813-817
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Science. ISSN 0036-8075 (print), 1095-9203 (online)