## Abstract Conformational studies of the three homologous series, from dimer through heptamer, of monodisperse, N‐and C‐protected oligopeptides derived from the γ‐branched α‐amino acid residues L‐leucine, β‐cyclohexyl‐L‐alanine, and L‐phenylalanine are reported. By means of ir absorption and CD in
Influence of the nature of the aromatic side-chain on the conductance of the channel of linear gramicidin: study of a series of 9,11,13,15-Tyr(O-protected) derivatives
✍ Scribed by D. Benamar; P. Daumas; Y. Trudelle; B. Calas; R. Bennes; F. Heitz
- Publisher
- Springer
- Year
- 1993
- Tongue
- English
- Weight
- 580 KB
- Volume
- 22
- Category
- Article
- ISSN
- 1432-1017
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✦ Synopsis
Thas paper describes the single channel properties of a series of synthetic analogues of gramicidin A, where all four tryptophans are replaced either by tyrosine or by several O-protected (benzyl, methyl, ethyl or tbutyl) derivatives. It as shown that, although all analogues bear similar dipole moment on their side-chains, the conductance depends on the hydrophobicity of these protecting groups. An analysis of the conductance data suggests that the conductance is governed by the binding process and a possible explanation, based on conformational considerations, is proposed.
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