中文摘要
生物模型分子体系的分子间相互作用研究是热力学研究的前沿领域。疏水相互作用是蛋白质等生物大分子维系其高级结构的一种重要的非键作用力。本项目拟以各种侧链结构的N-乙酰氨基酸、烷基取代酰胺、烷基取代脲、直链和支链脂肪醇以及带芳环的水溶性有机化合物等作为不同系列的疏水模型分子，以精密的流动微热量计作为测试手段，测定其水溶液的稀释焓、混合焓，计算同系和异系焓对作用系数，分析分子间发生对相互作用的优先构型及其影响因素，着重探讨分子中邻近官能团对疏水相互作用（尤其是疏水性的芳环堆积作用）的影响规律。在此基础上，重点构建一种新的基于焓效应的疏水性热力学尺度，用于预测蛋白质分子中氨基酸残基的疏水/亲水作用。有关研究对深入阐明疏水作用的热力学本质和机制，以及对研究和预测蛋白质的折叠构象稳定性具有重要意义。
英文摘要
The study on interactions between biological model molecule systems is an interesting field of thermodynamics.Hydrophobic interaction is an important nonbonding interaction force which is related to the holding of higher structure of biological molecules such as proteins. In this project, we select N-acetyl amino acids, α-amino alkyl alcohols, ringed alkyl alcohols, ringed alkyl amines, quadruple peptides of the same amino acid composition but of different sequence structure,and some organic compounds of aryl groups as the model molecules. Dilution enthalpes and mixing enthalpies of aqueous solutions of these compounds are planed to be determined.Homotactic and heterotactic enthalpic interaction coefficients are to be calculated. The preferential configuration of pairwise interaction, stereochemistry effects, rigid ring effects and chiral recognization effects between hydrated solute molecules are to be analyzed. The influences of the sequence of amino acids and the existing of adjacent functional groups on hydrophobic interaction, especially the hydrophobic π-π stacking interactions are to be explored. On the basis of that, we focus on the construction of a hydrophobility scale based on enthalpic effects, which can be applied to estimate the hydrophobic interactions in folding of proteins. The involved research is of special importance to clarify the thermodynamic mechanism of hydrophobic interactions,and the stability of folded configuration of proteins.
结题摘要
生物模型分子体系的分子间相互作用研究是热力学研究的前沿领域。疏水相互作用是蛋白质等生物大分子维系其高级结构的一种重要的非键作用力。本项目拟以各种侧链结构的N-乙酰氨基酸、烷基取代酰胺、烷基取代脲、直链和支链脂肪醇以及带芳环的水溶性有机化合物等作为不同系列的疏水模型分子，以精密的流动微热量计作为测试手段，测定其水溶液的稀释焓、混合焓，计算同系和异系焓对作用系数，分析分子间发生对相互作用的优先构型及其影响因素，着重探讨分子中邻近官能团对疏水相互作用（尤其是疏水性的芳环堆积作用）的影响规律。在此基础上，重点构建一种新的基于焓效应的疏水性热力学尺度，用于预测蛋白质分子中氨基酸残基的疏水/亲水作用。有关研究对深入阐明疏水作用的热力学本质和机制，以及对研究和预测蛋白质的折叠构象稳定性具有重要意义。