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 Scopus citations

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

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

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