| 光谱学与光谱分析 |
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| Study of Protein Conformation in Solution by Tyrosine Residues RRS Spectrum |
| ZHANG Yuan, LIN Zhe-xuan, LI Hui,LUO Wen-hong* |
| Central Laboratory, Shantou University Medical College, Shantou 515041, China |
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Abstract Due to the interference caused by the emission of tryptophan residue, it is hard to use fluorospectrophotometry to detect the spectrometric changes of the tyrosine residue when protein conformation is changed. When the concentration of protein in solution is relatively high, tyrosine residue has a characteristic scattering peak when excited with its K-band wavelength of light. In the present study, the authors established a method for detecting protein conformation changes in solution through the changes (peak height and wavelength shift) of the characteristic scattering peak of tyrosine residue. The method may be used for detecting protein conformation changes in solution caused by the changes of electrolyte, pH, and temperature.
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Received: 2005-09-06
Accepted: 2005-12-10
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Corresponding Authors:
LUO Wen-hong
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| Cite this article: |
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ZHANG Yuan,LIN Zhe-xuan,LI Hui, et al. Study of Protein Conformation in Solution by Tyrosine Residues RRS Spectrum[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(11): 2089-2092.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I11/2089 |
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