NDLI: Tertiary structure of H-Pro-Leu-Gly-NH2, the factor that inhibits release of melanocyte stimulating hormone, derived by conformational energy calculations.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ralston, E. Walter, R. De Coen, J. L.
Abstract	Conformational energy calculations were carried out on H-Pro-Leu-Gly-NH(2), the factor that inhibits the release of melanocyte stimulating hormone, and its biologically active analog, H-Pro-Ala-Gly-NH(2). Both peptides were found to be relatively compact molecules that retain, however, some degree of flexibility. After structure refinement, H-Pro-Leu-Gly-NH(2) 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 beta-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-NH(2) in dimethylsulfoxide and was also found by x-ray analysis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	71
Language	English
Publisher	National Academy of Sciences
Publisher Date	1974-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Oligopeptides Pituitary Hormone-Releasing Hormones Antagonists & Inhibitors Melanocyte-Stimulating Hormones Protein Conformation Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Tertiary structure of H-Pro-Leu-Gly-NH2, the factor that inhibits release of melanocyte stimulating hormone, derived by conformational energy calculations.