Dynamic and thermodynamic effects of glycerol on bovine serum albumin in aqueous solution: A tryptophan phosphorescence study

Sebastian Wachsmann-Hogiu, Mironel Enescu, Mihail Lucian Pascu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The phosphorescence decay of bovine serum albumin in water-glycerol solutions at room temperature is analysed by the maximum entropy method. While in pure water the decay was found to be quasi-monoexponential, in water-glycerol mixtures it is associated with more complex lifetime distributions. This is a direct proof for the existence of multiple protein conformers. It was also found that the increase of the glycerol concentration induces a continuous shift of the lifetime pattern to longer lifetimes. This effect is analysed in connection with the coupling between the solvent viscosity and the internal protein mobility.

Original languageEnglish (US)
Pages (from-to)55-60
Number of pages6
JournalJournal of Photochemistry and Photobiology B: Biology
Volume40
Issue number1
DOIs
StatePublished - Aug 1997
Externally publishedYes

Fingerprint

phosphorescence
Phosphorescence
tryptophan
bovine serum albumin
Bovine Serum Albumin
glycerols
albumins
Glycerol
Thermodynamics
Tryptophan
thermodynamics
serums
aqueous solutions
glycerol
life (durability)
Water
deterioration
water
Maximum entropy methods
proteins

Keywords

  • Bovine serum albumin
  • Conformational changes
  • Glycerol
  • Maximum entropy method
  • Phosphorescence decay
  • Protein structure
  • Viscosity effect

ASJC Scopus subject areas

  • Plant Science
  • Bioengineering
  • Physical and Theoretical Chemistry

Cite this

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title = "Dynamic and thermodynamic effects of glycerol on bovine serum albumin in aqueous solution: A tryptophan phosphorescence study",
abstract = "The phosphorescence decay of bovine serum albumin in water-glycerol solutions at room temperature is analysed by the maximum entropy method. While in pure water the decay was found to be quasi-monoexponential, in water-glycerol mixtures it is associated with more complex lifetime distributions. This is a direct proof for the existence of multiple protein conformers. It was also found that the increase of the glycerol concentration induces a continuous shift of the lifetime pattern to longer lifetimes. This effect is analysed in connection with the coupling between the solvent viscosity and the internal protein mobility.",
keywords = "Bovine serum albumin, Conformational changes, Glycerol, Maximum entropy method, Phosphorescence decay, Protein structure, Viscosity effect",
author = "Sebastian Wachsmann-Hogiu and Mironel Enescu and Pascu, {Mihail Lucian}",
year = "1997",
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T1 - Dynamic and thermodynamic effects of glycerol on bovine serum albumin in aqueous solution

T2 - A tryptophan phosphorescence study

AU - Wachsmann-Hogiu, Sebastian

AU - Enescu, Mironel

AU - Pascu, Mihail Lucian

PY - 1997/8

Y1 - 1997/8

N2 - The phosphorescence decay of bovine serum albumin in water-glycerol solutions at room temperature is analysed by the maximum entropy method. While in pure water the decay was found to be quasi-monoexponential, in water-glycerol mixtures it is associated with more complex lifetime distributions. This is a direct proof for the existence of multiple protein conformers. It was also found that the increase of the glycerol concentration induces a continuous shift of the lifetime pattern to longer lifetimes. This effect is analysed in connection with the coupling between the solvent viscosity and the internal protein mobility.

AB - The phosphorescence decay of bovine serum albumin in water-glycerol solutions at room temperature is analysed by the maximum entropy method. While in pure water the decay was found to be quasi-monoexponential, in water-glycerol mixtures it is associated with more complex lifetime distributions. This is a direct proof for the existence of multiple protein conformers. It was also found that the increase of the glycerol concentration induces a continuous shift of the lifetime pattern to longer lifetimes. This effect is analysed in connection with the coupling between the solvent viscosity and the internal protein mobility.

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KW - Glycerol

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KW - Phosphorescence decay

KW - Protein structure

KW - Viscosity effect

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