Tertiary Structure of H-Pro-Leu-Gly-NH2, the Factor That Inhibits Release of Melanocyte Stimulating Hormone, Derived by Conformational Energy Calculations
AUTOR(ES)
Ralston, Evelyn
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388179Documentos Relacionados
- Theoretical studies on pro-leu-gly-nh2 conformation.
- Regulation of Formation and Proposed Structure of the Factor Inhibiting the Release of Melanocyte-Stimulating Hormone
- Refinement of the X-ray Structure of Rubredoxin by Conformational Energy Calculations
- Structure of poly 8-bromoadenylic acid; conformational studies by CPF energy calculations.
- Glycine-directed peptide amidation: presence in rat brain of two enzymes that convert p-Glu-His-Pro-Gly-OH into p-Glu-His-Pro-NH2 (thyrotropin-releasing hormone).
