- PII
- S0006302925020031-1
- DOI
- 10.31857/S0006302925020031
- Publication type
- Article
- Status
- Published
- Authors
- Volume/ Edition
- Volume 70 / Issue number 2
- Pages
- 240-250
- Abstract
- The temperature dependence of the tryptophan fluorescence lifetime in human and bovine serum albumin in an aqueous solution and glycerol in the temperature range of –170°C to 20°C was studied. A model of forward and reverse electronic transitions in the tryptophan molecule from the excited state to the ground state and to the charge transfer state was constructed. Three main spectral regions of tryptophan fluorescence with different behavior of temperature dependences of transition rates from the excited state of tryptophan to the state with charge transfer were determined. It was found that the dynamics of the hydrogen bonding system in the selected spectral regions had a determining influence on the character of changes in the duration of tryptophan fluorescence. The nonlinear dependence of intramolecular transition rates on temperature found in the work is determined by the interaction of tryptophan molecules with its microenvironment. The rearrangements in the hydrogen bonding system of albumin protein containing tryptophan molecule have a determining influence on the processes of excitation deactivation in tryptophan.
- Keywords
- человеческий сывороточный альбумин бычий сывороточный альбумин триптофан флуоресценция
- Date of publication
- 24.10.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 17
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