Conformation-Directing Effects in Flexible Molecules

柔性分子中的构象导向效应

• 批准号: 9224561
• 负责人: Samuel Gellman
• 金额: $ 19.8万
• 依托单位: University of Wisconsin-Madison
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-04-01 至 1997-03-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9224561&HistoricalAwards=false
• 关键词: Conformation; Directing; Effects; Flexible; Molecules

This grant from the Organic Dynamics Program supports the work of Professor Gellman at the University of Wisconsin, Madison. This study will investigate the conformation-directing effects of intramolecular hydrogen bonds that are relevant to protein folding by 1H NMR and IR spectroscopic methods. The specific topics of study are: the intrinsic stability of isolated alpha-helical turns, the postulated helix-initiating role of N-terminal proline residues, the intrinsic stability of beta-hairpins, conformation-specifying effects of ionic peptide appendages, mechanisms of cooperativity among intramolecular hydrogen bonds, and the conformation-directing role of nonpolar-nonpolar interactions (including the hydrophobic effect) in aqueous solution. %%% The results from Professor Samuel H. Gellman's spectroscopic studies will contribute significantly to our understanding of protein folding. The importance of his work is the determination of thermodynamic parameters to assess the relative contributions of hydrophobicity and hydrogen bonding to peptide and protein stability.

有机动力学计划的这笔赠款支持以下工作： 麦迪逊的威斯康星州大学的盖尔曼教授。这 研究将调查构象导向效应 与蛋白质折叠相关的分子内氢键 通过~ 1H NMR和IR光谱方法。具体研究课题 是：孤立的α-螺旋圈的内在稳定性， 假定的N-末端脯氨酸残基的螺旋起始作用， β-发夹的内在稳定性，构象特异性 离子肽附件的作用，协同作用机制 分子内氢键之间，以及构象导向 非极性-非极性相互作用（包括疏水作用）的作用 效果）在水溶液中。 %%% 塞缪尔·H.盖尔曼分光 研究将大大有助于我们了解 蛋白质折叠他工作的重要性在于 热力学参数，以评估相对贡献 疏水性和与肽和蛋白质的氢键 稳定