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Conformational studies on the gramicidin A transmembrane channel in lipid micelles and liposomes

✍ Scribed by Masotti, Lanfranco ;Spisni, Alberto ;Urry, Dan W.


Book ID
112895149
Publisher
Springer-Verlag
Year
1980
Tongue
English
Weight
475 KB
Volume
2
Category
Article
ISSN
0163-4992

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## Abstract The present study investigated the effect of temperature and lipid/peptide molar ratio on the conformational changes of the membrane peptide gramicidin A from a double‐stranded helix to a single‐stranded helical dimmer in 1,2‐dimyristoyl‐glycerol‐3‐phosphochloine (DMPC) vesicles. Trypto

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## Abstract Conformational energy calculations are presented for the head‐to‐head dimerized β helices for Gramicidin A transmembrane channel structures. The calculations take into account both left‐ and right‐handed β helices, and various side‐chain conformations. The energetics of the dimerization