Experimentally, protein engineering and phi-value analysis is the method of choice to characterize the structure in folding transition state ensemble (TSE) of any protein. Combining experimental phi values and computer simulations has led to a deeper understanding of how proteins fold. In this report, we construct the TSE of chymotrypsin inhibitor 2 from published phi values. Importantly, we ve...

The dependence of the catalytic activities of α-chymotrypsin on the concentration of organic cosolvents (acetonitrile, dimethyl sulfoxide, dimethyl formamide, ethylene glycol, methanol, ethanol, propan-2-ol and tert-butanol) in mixed aqueous media has been studied towards hydrolysis of p-nitrophenyl acetate and p-nitrophenyl benzoate using cetyltriphenylphosphonium bromide surfactant at pH 7.75...

The stereochemical features of 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid and the N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide polypeptide substrate were investigated by nuclear magnetic resonance spectroscopy. Proton selective relaxation parameters gave the basis for the inhibitory activity of resorcin[4]arene in the hydrolysis of the polypep...

Chymotrypsin, trypsin, and Novo and Carlsberg subtilisins undergo a reversible, time-dependent inhibition by phenylarsonates. The inhibition of these enzymes by p-nitro-, p-tolyl-, p-aminophenyl-, and phenylarsonate was studied in detail, as a function of pH and inhibitor concentration, by a variety of approaches. KI values were determined for the inhibition of chymotrypsin and the subtilisins ...

1. A method is described for the purification of a proteinase, present in human seminal plasma and previously shown to accelerate migration of spermatozoa through cervical mucus in vitro. A 25-fold purification was achieved in three steps, consisting of ammonium sulphate fractionation, chromatography on CM-cellulose and gel filtration. 2. The enzyme displays some properties similar to chymotryp...

This paper reports on the presence of a strong binding site for the dye Biebrich Scarlet, (6-[Z-hydroxy-l-naphthyl]azo)3,4’-azodibenzene sulfonic acid, on cr-chymotrypsin. The 1: 1 protein-dye complex is characterized by a Kdiss of 8.8 f 0.1 X 10U5 M in 0.1 M phosphate buffer at pH 7.6 and W’. Complex formation is associated with a red shift in the visible spectrum of the dye, and a characteris...