THEORETICAL STUDIES ON THE DYNAMIC ASPECTS OF MACROMOLECULAR FUNCTION

非绝热电子转移速率的分子理论是 并建立了它与经典马库斯理论的联系。 研究发现，这一速度是由 能隙，定义为溶剂化过程中的瞬时变化 电子从施主向受主移动时的能量。确实是 展示了如何从自由能获得这个概率密度 在供体和受体之间转移不同数量的电荷 (由充电参数指定)。提出了一种简单的算法 用来计算这些自由能变化(以及由此产生的能隙 概率密度)来自计算机模拟的仅三种状态； 反应物、产物和通过转移一种 从施主到受主的正单位电荷。马库斯关系 (即，作为自由能的抛物线函数的激活能 反应的改变)以一种清楚地表明它是 在正常区域内即使在溶剂反应时也有很好的近似 是显著的非线性。简单地概括一下这个关系， 其中，激活能由抛物线函数给出，其中 提出了正常区域和倒置区域不同的曲率。 提出了一种分析核磁共振弛豫实验的新方法 在未折叠蛋白质上。它展示了光谱密度函数是如何 对酰胺键向量动力学的描述可在 仅使用N15弛豫参数的特定频率。实验 关于小蛋白折叠和未折叠形式的数据被用来 建立该程序的有效性--一个连续统模型 蛋白质中的静电相互作用已经被用来分析 分子内位置无序水分子的能量学 蛋白质表面上疏水的空腔，如最近结合的 实验中使用的是核磁共振。

A Molecular theory for the rate of nonadiabatic electron transfer was developed and its relation to classical Marcus theory was established. The rate was found to be determined by the probability density of the energy gap, which is defined as the instantaneous change in solvation energy upon moving an electron from the donor to the acceptor. It was shown how this probability density can be obtained from the free energies of transferring varying amounts of charge between the donor and acceptor (as specified by a charging parameter). A simple algorithm was proposed for calculating these free-energy changes (and hence the energy gap probability density) from computer simulations on just three states; the reactant,t he product, and an "anti" product formed by transferring a positive unit charge from the donor to the acceptor. The Marcus relation (i.e., the activation energy as a parabolic function of the free-energy change of reaction) was derived in a way that clearly shows that it is a good approximation in the normal region even when the solvent response is significantly nonlinear. A simple generalization of this relation, in which the activation energy is given by parabolic functions with different curvatures in the normal and inverted regions, was proposed. A novel method has been developed to analyze NMR relaxation experiments on unfolded proteins. It was shown how the spectral density function describing the dynamics of amide bond vectors can be determined at specific frequencies using N15 relaxation parameters alone. Experimental data on the folded and unfolded forms of a small protein was used to establish the validity of this procedure A continuum model of electrostatic interactions in protein has been used to analyze the energetics of a positionally disordered water molecule within an apparently hydrophobic cavity of a protein, as has recently been bound experimentally using NMR.