Conformation of Beta-endorphin and Beta-lipotropin: Formation of Helical Structure in Methanol and Sodium Dodecyl Sulfate Solutions

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1977 Aug 1

PMID 269386

Citations 9

Authors

J T Yang

T A Bewley

G C Chen

C H Li

Affiliations

Soon will be listed here.

Abstract

Circular dichroic spectra of camel beta-endorphin and ovine beta-lipotropin in water show little, if any, secondary structure. Intrinsic viscosities and sedimentation coefficients of the two peptides also suggest that the molecules are not compact and globular. Methanol or sodium dodecyl sulfate promotes the formation of helical structure to an extent as much as one-half of either peptide molecule. The conformation of the complex between camel beta-endorphin and dodecyl sulfate may be related to the opiate-like function of this peptide hormone.

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