THEORETICAL STUDY OF H BOND ENERGIES IN FINITE BONDING CHAINS OF AMIDES

这个项目的主要目的是提供合作氢键的数据，可以用来改进蛋白质折叠的理论方法。将对包括基集叠加误差平衡校正在内的势面进行高级（后Hartree-Fock）计算。我们将考虑各种构象的小酰胺（甲酰胺）的有限聚集体，特别是那些在蛋白质中很重要的聚集体（即-螺旋和-片）。数据将被组织为h结合链中酰胺的数量和六个分子间参数的函数，这些参数定义了每对相邻的甲酰胺的相互作用（一个距离，两个角度和三个二面体）。将经验函数拟合到数据中，目的是快速，准确地估计不同环境下的氢键相互作用。要注意消除对氢键能影响不大的参数。所得的经验函数可用于研究蛋白质折叠动力学。

The major purpose of this project is to provide data on cooperative hydrogen bonding that can be used to improve theoretical approaches to protein folding. High level (post Hartree-Fock) calculations on a potential surface that includes the counterpoise correction for basis set superposition error will be performed. We shall consider finite aggregates of small amides (formamide) in various conformations, particularly those that are important in proteins (i.e. alpha-helices and beta-sheets). The data will be organized as a function of the number of amides in the H-binding chain and the six intermolecular parameters that define the interaction of each pair of adjacent formamides (one distance, two angles, and three dihedrals). Empirical functions will be fitted to the data with the goal of rapidly, and accurately, estimating the H-bonding interactions for different environments. Care will be taken to eliminate whichever parameters have little effect upon the H-bonding energies. The resulting empirical functions can be used to study the dynamics of protein folding.