Tertiary structures of gastrin-like tetrapeptides.
Yamada, T., Wako, H., Saito, N., Isogai, Y.,  & Watari, H.
Int. J. Pept. Protein Res. (1976) 8, 607-614.

Abstract
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 ƒ¿-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.

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