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 α‐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.
|Number of pages||8|
|Journal||International Journal of Peptide and Protein Research|
|Publication status||Published - 1976 Nov|
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