Conformational Stability of Bovine Serum Albumin in Aqueous Amides: A Further Insight into the Mechanism of Urea Acting on the Protein |
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Authors: | Ma Lin Liu Chunli Huang Aimin Liao Dankui Yang Hua He Weiren Wei Qiaona |
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Institution: | 1. Tel.: 0086‐0771‐3233718;2. Fax: 0086‐0771‐3233718;3. Department of Chemistry and Chemical Engineering, Zaozhuang University, Zaozhuang, Shandong 277160, China;4. College of Chemistry and Chemical Engineering, Guangxi University, Nanning, Guangxi 530004, China |
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Abstract: | 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 NH2 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 NH2 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. |
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Keywords: | amide conformational stability fluorescence spectroscopy |
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