The Gramicidin A Transmembrane Channel: Characteristics of Head-to-Head Dimerized π(L,D)Helices
✍ Scribed by D. W. Urry, M. C. Goodall, J. D. Glickson and D. F. Mayers
- Book ID
- 123650730
- Publisher
- National Academy of Sciences
- Year
- 1971
- Tongue
- English
- Weight
- 688 KB
- Volume
- 68
- Category
- Article
- ISSN
- 0027-8424
- DOI
- 10.2307/61311
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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
In chloroform solution, the D,L-alteI'nating stereo-co-oligopeptide HCO-L-Phe-(DPhe-L-Phe),-OMe (I) forms three major species, two of which are dimeric and one tetrameric. One of the two dimeric species gives a specific set of 'H-nmr signals at 25°C; the other, together with the tetrameric species,