Ultraviolet Fluorescence of Proteins: Influence of Conformation and Environment.

摘要

The influence of variations in solvent composition upon the ultraviolet fluorescence of tryptophan-containing proteins is strongly dependent upon their conformation. In general, the response to the addition of neutral solvent increases under conditions where the organized structure is lost. The intensity of fluorescence is in general altered by conformational changes and may be used to monitor such changes. Rate constants computed in this way agree with those obtained from other criteria. Three examples are given. (Author)