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Influence of local interactions on protein structure. IV. Conformational energy studies of N ‐acetyl‐ N ′‐mehylamides of Ser‐X‐ and X‐Ser dipeptides
Author(s) -
Zimmerman S. Scott,
Scheraga Harold A.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170806
Subject(s) - chemistry , dipeptide , residue (chemistry) , peptide , stereochemistry , crystallography , organic chemistry , biochemistry
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.