Separation and analysis of dynamic stokes shift with multiple fluorescence environments: Coumarin 153 in bovine β-lactoglobulin A

Jeremy Pronchik, Jason T. Giurleo, David S. Talaga

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, β-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We develop a method to decompose the static and dynamic contributions to the spectral heterogeneity. This method is applied to temperature-dependent steady-state fluorescence spectra providing us with site-specific information about thermodynamic transitions in β-lactoglobulin. We confirm previously reported transitions and discuss the presence of an unreported transition of the central calyx at 18°C. Our method also resolves the contributions to the TDFSS from the coumarin 153 centrally located in the calyx of β-lactoglobulin despite overlapping signals from solvent exposed dyes. Our experiments show dynamics ranging from 3-1200 ps. The analysis shows a decrease in the encapsulated dye's heterogeneity during the relaxation, which is taken as evidence of the breakdown of linear response.

Original languageEnglish
Pages (from-to)11422-11434
Number of pages13
JournalJournal of Physical Chemistry B
Volume112
Issue number36
DOIs
StatePublished - 11 Sep 2008

Fingerprint

Lactoglobulins
Fluorescence
fluorescence
shift
Coloring Agents
Dyes
dyes
Lipocalins
Fluorophores
breakdown
Thermodynamics
thermodynamics
Molecules
coumarin 153
molecules
Experiments
Temperature
temperature

Cite this

@article{ad45e24b9a9142e3962d952857c0a463,
title = "Separation and analysis of dynamic stokes shift with multiple fluorescence environments: Coumarin 153 in bovine β-lactoglobulin A",
abstract = "We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, β-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We develop a method to decompose the static and dynamic contributions to the spectral heterogeneity. This method is applied to temperature-dependent steady-state fluorescence spectra providing us with site-specific information about thermodynamic transitions in β-lactoglobulin. We confirm previously reported transitions and discuss the presence of an unreported transition of the central calyx at 18°C. Our method also resolves the contributions to the TDFSS from the coumarin 153 centrally located in the calyx of β-lactoglobulin despite overlapping signals from solvent exposed dyes. Our experiments show dynamics ranging from 3-1200 ps. The analysis shows a decrease in the encapsulated dye's heterogeneity during the relaxation, which is taken as evidence of the breakdown of linear response.",
author = "Jeremy Pronchik and Giurleo, {Jason T.} and Talaga, {David S.}",
year = "2008",
month = "9",
day = "11",
doi = "10.1021/jp802666n",
language = "English",
volume = "112",
pages = "11422--11434",
journal = "Journal of Physical Chemistry B",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "36",

}

Separation and analysis of dynamic stokes shift with multiple fluorescence environments : Coumarin 153 in bovine β-lactoglobulin A. / Pronchik, Jeremy; Giurleo, Jason T.; Talaga, David S.

In: Journal of Physical Chemistry B, Vol. 112, No. 36, 11.09.2008, p. 11422-11434.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Separation and analysis of dynamic stokes shift with multiple fluorescence environments

T2 - Coumarin 153 in bovine β-lactoglobulin A

AU - Pronchik, Jeremy

AU - Giurleo, Jason T.

AU - Talaga, David S.

PY - 2008/9/11

Y1 - 2008/9/11

N2 - We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, β-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We develop a method to decompose the static and dynamic contributions to the spectral heterogeneity. This method is applied to temperature-dependent steady-state fluorescence spectra providing us with site-specific information about thermodynamic transitions in β-lactoglobulin. We confirm previously reported transitions and discuss the presence of an unreported transition of the central calyx at 18°C. Our method also resolves the contributions to the TDFSS from the coumarin 153 centrally located in the calyx of β-lactoglobulin despite overlapping signals from solvent exposed dyes. Our experiments show dynamics ranging from 3-1200 ps. The analysis shows a decrease in the encapsulated dye's heterogeneity during the relaxation, which is taken as evidence of the breakdown of linear response.

AB - We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, β-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We develop a method to decompose the static and dynamic contributions to the spectral heterogeneity. This method is applied to temperature-dependent steady-state fluorescence spectra providing us with site-specific information about thermodynamic transitions in β-lactoglobulin. We confirm previously reported transitions and discuss the presence of an unreported transition of the central calyx at 18°C. Our method also resolves the contributions to the TDFSS from the coumarin 153 centrally located in the calyx of β-lactoglobulin despite overlapping signals from solvent exposed dyes. Our experiments show dynamics ranging from 3-1200 ps. The analysis shows a decrease in the encapsulated dye's heterogeneity during the relaxation, which is taken as evidence of the breakdown of linear response.

UR - http://www.scopus.com/inward/record.url?scp=52349102514&partnerID=8YFLogxK

U2 - 10.1021/jp802666n

DO - 10.1021/jp802666n

M3 - Article

C2 - 18707077

AN - SCOPUS:52349102514

VL - 112

SP - 11422

EP - 11434

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

SN - 1520-6106

IS - 36

ER -