Abstract

The spectral-kinetic characteristics of the fluorescence of the tryptophan molecule in an aqueous solution and in the composition of a protein (albumin) were studied in the temperature range from –170 to 25°C. To explain the observed changes in the spectra and the tryptophan fluorescence lifetime with temperature, a model of transitions between the excited and ground states involving a charge-transfer state was used, which takes into account the nonlinear nature of the dynamics of these transitions. In these processes, an important role is played by the interaction of tryptophan molecules with its microenvironment, as well as rearrangements in the system of hydrogen bonds of the water–protein matrix surrounding the tryptophan molecule.

中文翻译：

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色氨酸荧光寿命的温度依赖性作为其微环境动力学的指标

摘要

在 –170 至 25°C 的温度范围内研究了水溶液中和蛋白质（白蛋白）组成中色氨酸分子荧光的光谱动力学特性。为了解释观察到的光谱变化和色氨酸荧光寿命随温度的变化，使用了涉及电荷转移状态的激发态和基态之间的跃迁模型，该模型考虑了这些跃迁动力学的非线性特性。在这些过程中，色氨酸分子与其微环境的相互作用以及色氨酸分子周围的水-蛋白质基质的氢键系统中的重排发挥了重要作用。