Fluorescence kinetics of tryptophan in a heterogeneous environment

Olaf J Rolinski, Vladislav Vyshemirsky

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Abstract

The potentially highly informative, but complex fluorescence decay of amino acids in protein is not fully understood and presents a barrier to understanding. Here we have tested a new and general approach to describing experimentally measured the fluorescence decay in a heterogeneous macroscopic sample. The decay parameters carry information on the features of the kinetics induced by the environment's heterogeneity. Bayesian interference demonstrated that the model fits well to the fluorescence decay of tryptophan in human serum albumin (HSA). The approach has the potential to accelerate photophysical research of heterogeneous media and, specifically, to solve a critical outstanding problem in interpreting protein fluorescence, paving the way to further progress in biomedical research.
Original languageEnglish
Article number045002
Number of pages14
JournalMethods and Applications in Fluorescence
Volume2
Issue number4
Early online date12 Dec 2014
DOIs
Publication statusPublished - 12 Dec 2014

Keywords

  • protein fluorescence
  • rotamer model
  • dielectric relaxation model
  • non-Debye kinetics
  • human serum albumin

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