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. 1977 Aug;74(8):3235–3238. doi: 10.1073/pnas.74.8.3235

Conformation of beta-endorphin and beta-lipotropin: formation of helical structure in methanol and sodium dodecyl sulfate solutions.

J T Yang, T A Bewley, G C Chen, C H Li
PMCID: PMC431512  PMID: 269386

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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