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Conformational Stability of Bovine Serum Albumin in Aqueous Amides: A Further Insight into the Mechanism of Urea Acting on the Protein
Author(s) -
Ma Lin,
Liu Chunli,
Huang Aiming,
Liao Dankui,
Yang Hua,
He Weiren,
Wei Qiaona
Publication year - 2010
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.201090164
Subject(s) - chemistry , hydrogen bond , formamide , urea , bovine serum albumin , aqueous solution , intramolecular force , amide , quenching (fluorescence) , fluorescence , acceptor , hydrophobic effect , crystallography , stereochemistry , organic chemistry , chromatography , molecule , physics , quantum mechanics , condensed matter physics
The binding distances of fluorescein to bovine serum albumin (BSA) in formamide‐water and N , N ‐dimethyl‐ formamide‐water mixtures were determined by fluorescence quenching method and compared with the values in urea‐water mixtures in our previous work. The results, together with the analysis of fluorescence spectra, were utilized to probe the conformational stability of protein in aqueous amides, providing a further insight into the mechanism of urea acting on protein. The spectral properties of BSA showed significant difference in the aqueous solutions of the three kinds of amide and indicated that both NH 2 group and C=O group could form hydrogen bond with the protein, serving as donor and acceptor, respectively. However, the results revealed that the multiple hydrogen bonds of NH 2 group with back bond and hydrophilic side chains of the protein played a key role in the nonspecific urea‐mediated network of intramolecular interaction due to its higher hydrogen bonding capability compared to C=O group.