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

这个项目的主要目的是提供关于合作氢键的数据，这些数据可以用来改进蛋白质折叠的理论方法。将在潜在表面上进行高水平(后Hartree-Fock)计算，其中包括对基组叠加误差的平衡校正。我们将考虑小酰胺(甲酰胺)在各种构象中的有限聚集体，特别是那些在蛋白质中重要的构象(即α-螺旋和β-折叠)。数据将根据H-结合链中的酰胺数量和定义每对相邻甲酰胺相互作用的六个分子间参数(一个距离、两个角度和三个二面体)来组织。经验函数将与数据进行拟合，目标是快速、准确地估计不同环境下的氢键相互作用。将注意消除任何对氢键能量影响很小的参数。由此得到的经验函数可用于研究蛋白质折叠的动力学。

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.