## 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
Head-to-head dimerization of parallel β helices in a synthetic model of the linear gramicidins
✍ Scribed by Gian Paolo Lorenzi; Christoph Gerber; Hans Jäckle
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 572 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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, gives another set of resonance signals. In a carbon tetrachloride or cyclohexane solution at 25"C, I forms virtually only the tetrameric species. From the nmr data, it can be shown that the dimeric and tetrameric species, that are in rapid equilibrium with each other in chloroform solutions, are a right-handed t tP5 helical dimer and the head-to-head (formylends-to-formylends) dimerization product of this dimer. It is suggested that the linear gramicidins may also form head-tohead dimers of parallel P helices, as observed for the model oligopeptide I.
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