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

酰胺有限键链氢键能的理论研究

• 批准号: 6450699
• 负责人: Joseph J Dannenberg
• 金额: $ 5.95万
• 依托单位: HUNTER COLLEGE
• 依托单位国家: 美国
• 财政年份: 2001
• 资助国家: 美国
• 起止时间: 2001-04-01 至 2002-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6450699
• 关键词: chemical models; computer simulation; energy source; formamide; hydrogen bond; intermolecular interaction; molecular dynamics; molecular orbital; protein folding

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.

该项目的主要目的是提供有关合作氢键的数据，该数据可用于改善理论方法的蛋白质折叠方法。将在包括基本集合置换误差的电平校正的潜在表面上进行高水平（Hartree fock后）计算。我们将考虑各种构象的小酰胺（甲酰胺）的有限聚集体，尤其是那些在蛋白质中很重要的构象（即α-螺旋和β-片）。数据将作为H结合链中酰胺数和六个分子间参数的函数组织，该参数定义了每对相邻的甲酰胺的相互作用（一个距离，两个角度和三个二二二二二二轴）。经验功能将拟合到数据，以快速，准确地估算不同环境的H键相互作用。将注意消除任何参数对H键能的影响几乎没有影响。所得的经验功能可用于研究蛋白质折叠的动力学。