title: Comparative theoretical conformational analysis of the insulin A6-A11 peptides.
abstract: The insulins of pig, ox, horse and goat differ only by the cyclic A6-A11 peptide which is thought to be an antigenic determinant of the molecule. The structure of the four peptides is investigated by conformational energy calculations in order to verify whether a common backbone conformation can be found for all four species, the antigenic difference being consequently due only to the difference in the side chains exposed to the solvent, or whether each sequence gives rise to a preferential backbone conformation, which would lead to the conclusion that the antigenic difference is conveyed by a more pronounced difference in the molecular structure. From the results of the study on the isolated peptides, it appears that an energetically favourable backbone conformation common to all four species can be found. This conformation is compared with the structure deduced from the X-ray diffraction data available for pig insulin.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006041:Goats; D006736:Horses; D007328:Insulin; D010446:Peptide Fragments; D011487:Protein Conformation; D013045:Species Specificity; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D007328:Insulin; D010446:Peptide Fragments