| 光谱学与光谱分析 |
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| Study on Interaction of Anionic Surfactant SDS and Bovine Serum Albumin by Fourier Transform Infrared Spectroscopy |
| WANG Jing1, 2, GUO Chen1, LIANG Xiang-feng1, 2, ZHENG Li-li1, 2, CHEN Shu1, 2, MA Jun-he1, 2, LIU Hui-zhou1* |
1. Young Scientist Laboratory of Separation Science and Engineering, State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, China
2. Graduate School of Chinese Academy of Sciences, Beijing 100039, China |
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Abstract FTIR spectroscopy was applied to investigate the interaction of anionic surfactant Sodium Dodecyl Sulfate (SDS) and Bovine Serum Albumin (BSA). Amide band Ⅰ of BSA was analyzed to obtain the change in secondary structure of BSA when different concentration of SDS was added and during different interaction period. In short interaction period and at low concentration of SDS, the α-helixes increased and the random coil decreased. In long interaction period or at high concentration of SDS, SDS unfolded the protein by decreasing the α-helix structure and increasing the random coil.
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Received: 2005-05-18
Accepted: 2005-08-08
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Corresponding Authors:
LIU Hui-zhou
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| Cite this article: |
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WANG Jing,GUO Chen,LIANG Xiang-feng, et al. Study on Interaction of Anionic Surfactant SDS and Bovine Serum Albumin by Fourier Transform Infrared Spectroscopy[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(09): 1598-1600.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I09/1598 |
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