Open AccessConformation of beta-endorphin and beta-lipotropin: formation of helical structure in methanol and sodium dodecyl sulfate solutions.
Author(s) -
Jen Tsi Yang,
Thomas A. Bewley,
G C Chen,
C H Li
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.8.3235
Subject(s) - sodium dodecyl sulfate , chemistry , peptide , beta (programming language) , molecule , beta endorphin , sodium , sulfate , globular protein , crystallography , stereochemistry , chromatography , biochemistry , organic chemistry , computer science , programming language
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.