Premium
Influence of the Mixing State of tert ‐Butyl Alcohol‐water Mixtures on the Conformation of Bovine Serum Albumin
Author(s) -
MA Lin,
WANG Xu,
XU Li,
HE WeiRen,
WEI ZhiQiang,
LIN RuiSen
Publication year - 2008
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200890323
Subject(s) - chemistry , bovine serum albumin , hydrate , ternary operation , molecule , crystallography , chromatography , analytical chemistry (journal) , organic chemistry , computer science , programming language
The hydrodynamic radii of bovine serum albumin (BSA) in TBA‐water mixtures were determined by dynamic light scattering measurements and utilized to investigate the conformational change of BSA in TBA‐water mixtures, together with the analysis of the fluorescence spectra and UV‐vis absorption spectra of BSA. Meanwhile, static light scattering measurements were used to probe the mixing state of the binary mixtures of TBA‐water and the ternary mixtures of BSA‐TBA‐water and its influence on the conformation of the protein. A close relationship between the mixing state of TBA‐water mixtures and the conformation of BSA was observed. The mixing state of TBA‐water mixture at a low concentration was characterized by the clathrate hydrate of TBA caged by water molecules and it was found that hydrophobic binding of TBA to nonpolar groups of BSA in general destabilized the native structure of the protein, however, addition of a small amount of TBA attenuated the hydrophobic interactions among nonpolar groups of the protein and promoted a more ordered conformation. The results clearly showed that clustering of TBA at a high concentration reduced the effectiveness on destabilization of the compact conformation of proteins.