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Polypeptide chains with similar amino acid sequences but a distinctly different conformation
Author(s) -
Dijkstra Bauke W.,
Weijer Wicher J.,
Wierenga Rik K.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80011-8
Subject(s) - folding (dsp implementation) , chemistry , residue (chemistry) , protein primary structure , structural similarity , stereochemistry , sequence (biology) , polypeptide chain , pancreatic polypeptide , disulfide bond , peptide sequence , amino acid , crystallography , biochemistry , hormone , glucagon , electrical engineering , gene , engineering
The primary structures of bovine and porcine pancreatic phospholipase A 2 differ only by about 15%. Nevertheless, a 12 residue loop, with only one substitution (Val→Phe) has a quite different conformation, whereas the rest of the molecules have a very similar folding indeed. From this observation it is concluded that prediction of a 3‐dimensional structure on the basis of sequence similarity of short segments alone might give erroneous results.