Evidence for tertiary structure in aqueous solutions of human .beta.-endorphin as shown by difference absorption spectroscopy
- 30 April 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (11) , 2671-2675
- https://doi.org/10.1021/bi00280a013
Abstract
The presence of a distinct tertiary structure in aqueous solutions of human .beta.-endorphin was demonstrated by difference absorption spectroscopy of thermolysin digests of the hormone and synthetic analogs. The .alpha.-amino group of Tyr1, Lys28 and some residue(s) between Thr6 and Ser110 are involved in forming and stabilizing the folded form of the molecule. Although a peptide corresponding to the first 9 residues of human .beta.-endorphin shows definite evidence of tertiary structure, the pentapeptide methionine-enkephalin does not.This publication has 0 references indexed in Scilit: