Evidence for tertiary structure in aqueous solutions of human beta-endorphin as shown by difference absorption...

The presence of a distinct tertiary structure in aqueous solutions of human beta-endorphin has been demonstrated by difference absorption spectroscopy of thermolysin digests of the hormone and synthetic analogues. The results demonstrate that the alpha-amino group of Tyr1, Lys28, and some residue(s) between Thr6 and Ser10 are involved in forming and stabilizing the folded form of the molecule. Although a peptide corresponding to the first nine residues of human beta-endorphin shows definite evidence of tertiary structure, the pentapeptide methionine-enkephalin does not.