Abstract
Theoretical conformational analysis was carried out for Ac-(Ala-Gly)12-NHMe, which was a model polypeptide of Bombyx mori silk fibroin, using ECEPP and the conformational energy minimization procedure. The hypothesis on the interaction in polypeptide molecules was also used for the analysis. Calculated results showed that right-handed α-helix and left-handed β4.6-helix were the lowest-energy and 2nd low-energy conformations, respectively. Several stable conformations, which were related to the already proposed model structures of silk fibroin, were also found in the theoretically obtained conformational ensemble of Ac-(Ala-Gly)12-NHMe.
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