Conformation-Directing Effects in Flexible Molecules

这项来自有机动力学项目的拨款支持威斯康辛大学麦迪逊分校Gellman教授的工作。本研究将通过1H NMR和IR光谱方法研究与蛋白质折叠相关的分子内氢键的构象引导作用。具体研究课题有：孤立的α -螺旋旋转的固有稳定性，n端脯氨酸残基的螺旋启动作用，β -发夹的固有稳定性，离子肽附件的构象指定作用，分子内氢键的协同作用机制，以及水溶液中非极性-非极性相互作用（包括疏水效应）的构象导向作用。塞缪尔·h·格尔曼教授的光谱研究结果将对我们对蛋白质折叠的理解作出重大贡献。他的工作的重要性在于确定热力学参数，以评估疏水性和氢键对肽和蛋白质稳定性的相对贡献。

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.