Tertiary structures of gastrin-like tetrapeptides.
Tertiary structures of gastrin-like tetrapeptide Trp-Met-Asp-Phe-NH2 and those substituted by Leu, Val or Gly for Met are studied. The lowest energy conformations of the side chains when the back bone is fixed in alpha-helix are obtained by modified minimization algorithm. It is suggested that protein folding proceeds in the accessible conformation space as a self-organization process leading to minimum energy conformation in this space.
D001224:Aspartic Acid; D005755:Gastrins / Q000032:analysis*; D005998:Glycine; D006860:Hydrogen Bonding; D007930:Leucine; D008715:Methionine; D008961:Models, Structural; D008968:Molecular Conformation; D010455:Peptides / Q000032:analysis*; D010649:Phenylalanine; D014364:Tryptophan; D014633:Valine
D005755:Gastrins; D010455:Peptides; D001224:Aspartic Acid; D010649:Phenylalanine; D014364:Tryptophan; D008715:Methionine; D007930:Leucine; D014633:Valine; D005998:Glycine