Alcala J R, Gratton E, Prendergast F G
Biophys J. 1987 Apr;51(4):597-604. doi: 10.1016/S0006-3495(87)83384-2.
The fluorescence lifetime value of tryptophan residues varies by more than a factor of 100 in different proteins and is determined by several factors, which include solvent exposure and interactions with other elements of the protein matrix. Because of the variety of different elements that can alter the lifetime value and the sensitivity to the particular environment of the tryptophan residue, it is likely that non-unique lifetime values result in protein systems. The emission decay of most proteins can be satisfactorily described only using several exponential components. Here it is proposed that continuous lifetime distributions can better represent the observed decay. An approach based on protein dynamics is presented, which provides fluorescence lifetime distribution functions for single tryptophan residue proteins. First, lifetime distributions for proteins interconverting between two conformations, each characterized by a different lifetime value, are derived. The evolution of the lifetime values as a function of the interconversion rate is studied. In this case lifetime distributions can be obtained from a distribution of rates of interconversion between the two conformations. Second, the existence of a continuum of energy substates within a given conformation was considered. The occupation of a particular energy substate at a given temperature is proportional to the Boltzmann factor. The density of energy states of the potential well depends upon the width of the well, which determines the degree of freedom the residue can move in the conformational space. Lifetime distributions can be obtained by association of each energy substate with a different lifetime value and assuming that the average conformation can change as the energy of the substate is increased. Finally, lifetime distributions for proteins interconverting between two conformations, each characterized by a quasi-continuum of energy substates, are presented. The origin of negative components of the lifetime distribution is also discussed. In the companion paper that will follow (Alcala, J. R., E. Gratton, and F. J.Prendergast, 1987, Biophys. J., in press) lifetime distributions obtained here are used to fit experimental data.
色氨酸残基的荧光寿命值在不同蛋白质中变化超过100倍,且由多种因素决定,这些因素包括溶剂暴露以及与蛋白质基质中其他元素的相互作用。由于多种不同元素可改变寿命值以及色氨酸残基对特定环境的敏感性,蛋白质系统中很可能会出现非唯一的寿命值。大多数蛋白质的发射衰减仅用几个指数成分就能得到令人满意的描述。本文提出连续寿命分布能更好地表示观测到的衰减。提出了一种基于蛋白质动力学的方法,该方法为单个色氨酸残基蛋白质提供荧光寿命分布函数。首先,推导了在两种构象之间相互转换的蛋白质的寿命分布,每种构象具有不同的寿命值。研究了寿命值随相互转换速率的变化。在这种情况下,寿命分布可从两种构象之间相互转换速率的分布中获得。其次,考虑了给定构象内存在连续的能量亚态。在给定温度下,特定能量亚态的占有率与玻尔兹曼因子成正比。势阱的能态密度取决于势阱的宽度,势阱宽度决定了残基在构象空间中移动的自由度。通过将每个能量亚态与不同的寿命值相关联,并假设平均构象会随着亚态能量的增加而变化,可得到寿命分布。最后,给出了在两种构象之间相互转换的蛋白质的寿命分布,每种构象的特征是能量亚态的准连续体。还讨论了寿命分布中负成分的起源。在随后的配套论文(阿尔卡拉,J.R.,E.格拉顿,和F.J.普伦德加斯特,1987,《生物物理杂志》待发表)中,这里获得的寿命分布用于拟合实验数据。