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Home / Protein and Peptide Letters, Volume 13, Number 4

Unfolding During Urea Denaturation of a Low Molecular Weight Phytocystatin (Thiol Protease Inhibitor) Purified from Phaseolus mungo (Urd)

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In the present study, two phytocystatins were purified to homogeneity as peaks I and II with molecular weights of 19 kDa and 17 kDa, respectively, as determined by SDS-PAGE and mass spectrometry. Both PMCs I and II were purified with a greater than 1000-fold purification and overall yield of about 16-18%. The effect of urea on PMC I and II was analysed by fluorescence and Circular Dichroism (CD) spectroscopy. Fluorescence studies suggest a red shift of the maximum emission at higher urea concentrations. PMC I and II are extremely stable protein inhibitors with regards to temperature and pH stability. FTIR studies show predominant a-helical structure in both the cystatins. CD analysis results show change in urea concentration-dependent loss in ellipticity, as well as in the shape of the CD spectrum compared to the intact phytocystatin.





Keywords: Circular Dichroism; Fluorescence Spectroscopy; Plant cystatins; Proteins; Purification; Thiol protease inhibitors

Document Type: Research Article

Affiliations: Department of Biochemistry, Faculty of Life, Sciences, Aligarh Muslim University, Aligarh-202002 (U.P.) India.

Publication date: 01 April 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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