前体亮氨酸-甘氨酸-氨基的构象的理论研究
Theoretical studies on pro-leu-gly-nh2 conformation.
作者信息
Kang S, Walter R
出版信息
Proc Natl Acad Sci U S A. 1976 Apr;73(4):1203-6. doi: 10.1073/pnas.73.4.1203.
Abstract
Classical potential function calculations were carried out on the hypothalamic factor Pro-Leu-Gly-NH2. The results indicate that the proposed 10-membered, hydrogen-bonded beta-turn conformation of this tripeptide is a strongly preferred structure. Its stability appears to be inherent in the rather rigid backbone conformation of the leucine residue rather than the hydrogen bond between the carboxamide proton of glycinamide and the C=O of the proline moiety; the glycinamide has little influence on the phi-psi of the leucine backbone structure. The type II beta-turn structure of the Pro-Leu-Gly-NH2 is preferred.
摘要
对下丘脑因子脯氨酸 - 亮氨酸 - 甘氨酸 - 酰胺进行了经典势函数计算。结果表明，该三肽所提出的具有氢键的10元β - 转角构象是一种强烈偏好的结构。其稳定性似乎源于亮氨酸残基相当刚性的主链构象，而非甘氨酰胺的酰胺质子与脯氨酸部分的C = O之间的氢键；甘氨酰胺对亮氨酸主链结构的φ - ψ几乎没有影响。脯氨酸 - 亮氨酸 - 甘氨酸 - 酰胺的II型β - 转角结构更受青睐。
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