Dynamic and thermodynamic effects of glycerol on bovine serum albumin in aqueous solution: a tryptophan phosphorescence study.
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.
Hogiu
S
S
Institute of Atomic Physics, Laser Department, Bucharest-Magurele, Romania.
Enescu
M
M
Pascu
M L
ML
D000818:Animals; D002417:Cattle; D019277:Entropy; D005990:Glycerol / Q000494:pharmacology*; D007700:Kinetics; D008163:Luminescent Measurements; D011487:Protein Conformation / Q000187:drug effects*; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000187:drug effects; D014364:Tryptophan
D012710:Serum Albumin, Bovine; D014364:Tryptophan; D005990:Glycerol