A method for determining states in the course of protein unfolding

作者: Mostafa Rezaei-Tavirani , Sayed-Amir Marashi , Seyed Mohammad Mahdavi

DOI: 10.17877/DE290R-122

关键词:

摘要: A simple model is presented for analyzing a set of spectra obtained from spectrophotometric study protein titration. With this one can determine the states (probable) intermediates in course unfolding. The developed based on abundance native state, intermediate(s) and denatured their contributions to differential absorbance at selected wavelengths. tested two-state unfolding ribonuclease by urea formate buffer, also three-state α-lactalbumin guanidine hydrochloride (GdnHCl) phosphate buffer. It was demonstrated that matched acceptably with model, while starts twostate mechanism (when [GdnHCl]≥1.6M) followed pathway.

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