研究目的
Investigating the interaction between brilliant blue and trypsin using fluorescent technique to understand the binding constants, thermodynamic parameters, and binding sites.
研究成果
The study concluded that the fluorescence quenching of trypsin by brilliant blue is static, with electrostatic interaction being the dominant force. The binding distance was determined using F?rster energy transfer theory, indicating a high possibility of energy transfer.
研究不足
The study is limited to the interaction between brilliant blue and trypsin under specific conditions (pH 7.24) and may not account for all possible interactions in different environments.
1：Experimental Design and Method Selection:
The interaction was studied using fluorescent technique with data analyzed according to Stern-Volmer and Lineweaver-Burk equations.
2：Sample Selection and Data Sources:
Trypsin and brilliant blue solutions were prepared in specific concentrations.
3：List of Experimental Equipment and Materials:
TU1901 UV-visible Spectrophotometer, F-4500 fluorescence spectrometer, PHS-23 meter.
4：Experimental Procedures and Operational Workflow:
Solutions were mixed, reacted, and then analyzed for fluorescence and absorption spectra.
5：Data Analysis Methods:
Data were processed using Stern-Volmer and Lineweaver-Burk equations to obtain binding constants and thermodynamic parameters.
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