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Functional stability and structural transitions of Kallikrein: spectroscopic and molecular dynamics studies
Kallikrein, a physiologically vital serine protease, was investigated for its functional and conformational transitions during chemical (organic solvents, Gdn-HCl), thermal, and pH induced denaturation using biochemical and biophysical techniques and molecular dynamics (MD) simulations approach. The enzyme was exceptionally stable in isopropanol and ethanol showing 110% and 75% activity, respectively, after 96 h, showed moderate tolerance in acetonitrile (45% activity after 72 h) and much lowerdoi:10.6084/m9.figshare.1632815.v2 fatcat:sl3is5mqprb63px3q3giai2ru4