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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📜 SIMILAR VOLUMES
## 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
## 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