Abstract
As one of the steps for investigating the conformational properties of the periodic poly(dipeptide)s composed of the Pro residue, theoretical conformational analysis was carried out for poly(Gly-Pro) using ECEPP and the conformational minimization procedure. Calculated results showed that right-handed β6.8-helix is the most stable helical conformation of poly(Gly-Pro). Obtained conformational preference of poly(Gly-Pro) indicates that poly(dipeptide)s composed of Pro residue can be expected as one of the useful periodic polypeptides for designing the functional polypeptides.
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