Tertiary Structure of H-Pro-Leu-Gly-NH 2 , the Factor That Inhibits Release of Melanocyte Stimulating Hormone, Derived by Conformational Energy Calculations
- 1 April 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (4), 1142-1144
- https://doi.org/10.1073/pnas.71.4.1142
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.Keywords
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