Kishner S, Trepman E, Galley W C
Can J Biochem. 1979 Nov;57(11):1299-304. doi: 10.1139/o79-173.
When tryptophyl side chains are hidden within relatively inflexible domains of globular proteins, the lifetime of the phosphorescence from these residues provides a measure of the local conformational flexibility. The phosphorescence decay from the tryptophan buried at the base of the nucleotide-binding domain in liver alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) was monitored between 1 and 40 degrees C to determine the energetics associated with the rate of local unfolding. The slow rate at which this process takes place is found to result from a high entropic barrier rather than from the disruption of strong intramolecular interactions. This observation along with the response of the system to solvent perturbations points to the significance of solvent-protein interactions in determining conformational flexibility.
当色氨酸侧链隐藏在球状蛋白质相对不灵活的结构域内时，这些残基磷光的寿命提供了局部构象灵活性的一种度量。监测了肝醇脱氢酶（醇：NAD+氧化还原酶，EC 1.1.1.1）核苷酸结合结构域底部埋藏的色氨酸在1至40摄氏度之间的磷光衰减，以确定与局部解折叠速率相关的能量学。发现这个过程发生的缓慢速率是由高熵垒导致的，而不是由于强分子内相互作用的破坏。这一观察结果以及系统对溶剂扰动的响应表明溶剂 - 蛋白质相互作用在决定构象灵活性方面的重要性。
