Model Studies on the Biostructural Role of Amide-Amide Hydrogen Bonds

在有机动力学项目的支持下，盖尔曼博士将评估涉及酰胺基团的氢键对决定球状蛋白质整体构象稳定性的贡献。该项目利用含有有限数量的酰胺基团的小而灵活的分子来剖析这一特定类别的非共价相互作用的贡献。这项工作的结果有望加深对决定蛋白质三维结构的因素的理解，从而指导球状蛋白质的生物功能(酶、调节或结构)。各种模型体系中的构象偏好将在内部氢键具有重要能量的条件下用光谱学进行研究。在一系列密切相关的寡酰胺中观察到的构象偏好应该提供有关氢键强度受键合伙伴的空间取向影响的方式的信息。这种分析还应该揭示氢键受到其他内部非共价相互作用的影响的方式，以及它们如何受到环境(例如，溶剂)的影响。

With support from the Organic Dynamics Program, Dr. Gellman will evaluate the contribution made by hydrogen bonds that involve amide groups toward determining the overall conformational stability of globular proteins. The project utilizes small, flexible molecules that contain a limited number of amide groups to dissect the contribution of this one particular class of non-covalent interaction. Results obtained from this work are expected to afford increased understanding of the factors that determine three-dimensional protein structure and, accordingly, that direct the biological function (enzymatic, regulatory or structural) of a globular protein. Conformational preferences in the various model systems will be studied spectroscopically under conditions in which internal hydrogen bonds are energetically significant. Conformational preferences observed in a series of closely related oligoamides should provide information about the manner in which hydrogen bond strength is affected by the spatial orientation of the bonding partners. This analysis also should reveal the manner in which hydrogen bonds are affected by other internal non-covalent interactions, and also how they are affected by the environment (e.g., solvent).