Fluorescence kinetics of tryptophan in a heterogeneous environment

Olaf J Rolinski, Vladislav Vyshemirsky

Research output: Contribution to journalArticle

5 Citations (Scopus)

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.
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

Fingerprint

tryptophan
Tryptophan
Fluorescence
fluorescence
Kinetics
kinetics
decay
proteins
Proteins
albumins
Serum Albumin
serums
amino acids
Amino acids
interference
Amino Acids

Keywords

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

Cite this

@article{037fc5a7331a4e74a25f16f11440ae6c,
title = "Fluorescence kinetics of tryptophan in a heterogeneous environment",
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.",
keywords = "protein fluorescence, rotamer model, dielectric relaxation model, non-Debye kinetics, human serum albumin",
author = "Rolinski, {Olaf J} and Vladislav Vyshemirsky",
year = "2014",
month = "12",
day = "12",
doi = "10.1088/2050-6120/2/4/045002",
language = "English",
volume = "2",
journal = "Methods and Applications in Fluorescence",
issn = "2050-6120",
number = "4",

}

Fluorescence kinetics of tryptophan in a heterogeneous environment. / Rolinski, Olaf J; Vyshemirsky, Vladislav.

In: Methods and Applications in Fluorescence , Vol. 2, No. 4, 045002, 12.12.2014.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Fluorescence kinetics of tryptophan in a heterogeneous environment

AU - Rolinski, Olaf J

AU - Vyshemirsky, Vladislav

PY - 2014/12/12

Y1 - 2014/12/12

N2 - 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.

AB - 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.

KW - protein fluorescence

KW - rotamer model

KW - dielectric relaxation model

KW - non-Debye kinetics

KW - human serum albumin

UR - http://iopscience.iop.org/2050-6120/

U2 - 10.1088/2050-6120/2/4/045002

DO - 10.1088/2050-6120/2/4/045002

M3 - Article

VL - 2

JO - Methods and Applications in Fluorescence

T2 - Methods and Applications in Fluorescence

JF - Methods and Applications in Fluorescence

SN - 2050-6120

IS - 4

M1 - 045002

ER -