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. 1974 Apr;71(4):1142–1144. doi: 10.1073/pnas.71.4.1142

Tertiary Structure of H-Pro-Leu-Gly-NH2, the Factor That Inhibits Release of Melanocyte Stimulating Hormone, Derived by Conformational Energy Calculations

Evelyn Ralston *,‡, Jean-Louis De Coen *,‡, Roderich Walter *
PMCID: PMC388179  PMID: 4598294

Abstract

Conformational energy calculations were carried out on H-Pro-Leu-Gly-NH2, the factor that inhibits the release of melanocyte stimulating hormone, and its biologically active analog, H-Pro-Ala-Gly-NH2. Both peptides were found to be relatively compact molecules that retain, however, some degree of flexibility. After structure refinement, H-Pro-Leu-Gly-NH2 possesses at least three preferred compact conformations. Two of these conformations occupy rather broad and flat energy troughs, while a third occupies a narrow and deep potential energy well. This third structure, which consists of a 10-membered β-turn closed by a (4 → 1) hydrogen bond between the proton of the trans carboxamide of Gly and the C=O of Pro, is the one that was proposed for H-Pro-Leu-Gly-NH2 in dimethylsulfoxide and was also found by x-ray analysis.

Keywords: conformation, conformation-activity relationship, hypothalamic factor

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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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