| Abstract: | Conformational energy calculations using an empirical conformatinol energy program for peptides (ECEPP) werer carried out on 16 N-acetyl-N′-methylamides of Ser-X and X- Ser dipeptides, where X = Ala, Asn, Asn, Asp, Gly, Phe, Ser, Thr, and Val, and on Pro-Ser. As with the other dipeptides studied in this serites, intraresidue interactions found to dominate over interresidue interactions in determining conformational properties. The Ser-containing dipeptides (except for those with a pro or Gly residue) were found to have unusually low calculated bend probailities, in disagreement observations on proteins; this discrepancy probably arises becuse of sovent effects (not included in the computations). The Ser-X dipeptides were calculated to have a lower preference for bends than the X-Ser dipeptides. |
