id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-255815-5d9bqji0	Malik, Ajamaluddin	MERS‐CoV papain-like protease (PL(pro)): expression, purification, and spectroscopic/thermodynamic characterization	2017-05-30		.txt	text/plain	3925	243	59	An orthogonal technique based on intrinsic tryptophan fluorescence also showed that MERS-CoV PL(pro) undergoes a single thermal transition and unfolds via a pathway of two-state folding with a T (m) value of 51.4 °C. In a similar experiment, MERS-CoV PL pro was gradually heated from 20 to 80°C at a rate of 1°C/min during which tryptophan fluorescence was measured by exciting at 295 nm and collecting at 330 and 350 nm to obtain the temperature melting curve. Commonly, protein unfolding fluorescence spectra are characterized by a long wavelength shift ''red-shift.'' But some proteins, Fig. 2 a Sequence of C-terminal His-tagged MERS-CoV PL pro showing ten Tyr and five Trp residues, which are highlighted in green and blue, respectively. Our result showed that the band intensity of the supernatant samples incubated from 20 to 70°C was apparently unchanged (Fig. 5) , indicating Fig. 3 Thermally induced structural changes in MERS-CoV PL pro as monitored by the intrinsic tryptophan fluorescence spectroscopy.	./cache/cord-255815-5d9bqji0.txt	./txt/cord-255815-5d9bqji0.txt