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

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 fl...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1974-04, Vol.71 (4), p.1142-1144
Main Authors: Ralston, Evelyn, De Coen, Jean-Louis, Walter, Roderich
Format: Article
Language:English
Subjects:
Amides
Biochemistry
Biological Sciences: Biophysics
Hormones
Hydrogen bonds
Melanocyte-Stimulating Hormones
Melanocytes
Oligopeptides
Permittivity
Pituitary Hormone-Releasing Hormones - antagonists & inhibitors
Protein Conformation
Protons
Rotation
Solvents
Spine
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Summary: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-NH2possesses at least three preferred compact conformations. Two of these conformations occupy rather broad and flat energy throughs, 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 [Note: See the image of page 1142 for this formatted text] C--O of Pro, is the one that was proposed for H-Pro-Leu-Gly-NH2in dimethylsulfoxide and was also found by x-ray analysis.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.71.4.1142