S
Shyamala Rajender
Researcher at University of Minnesota
Publications - 6
Citations - 1155
Shyamala Rajender is an academic researcher from University of Minnesota. The author has contributed to research in topics: Chymotrypsinogen & Substrate (chemistry). The author has an hindex of 5, co-authored 6 publications receiving 1099 citations.
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Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water.
Rufus Lumry,Shyamala Rajender +1 more
TL;DR: It is tentatively concluded that the pattern is real, very common and a consequence of the properties of liquid water as a solvent regardless of the solutes and the solute processes studied, and that liquid water plays a direct role in many protein processes and may be a common participant in the physiological function of proteins.
Journal ArticleDOI
Studies of the chymotrypsinogen family of proteins. XVI. Enthalpy-entropy compensation phenomenon of -chymotrypsin and the temperature of minimum sensitivity.
Rufus Lumry,Shyamala Rajender +1 more
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Modification of protein properties by change in charge. Succinylated chymotrypsinogen.
TL;DR: The pH dependence suggests that three ionizing groups influence catalytic behavior and succinylated chymotrypsin is active as an esterase with N-acetyl-l-tryptophan ethyl ester with a small decrease in the maximum-velocity parameter.
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Studies of the chymotrypsinogen family of proteins. IX. Steady-state kinetics of the chymotryptic hydrolysis of N-acetyl-L-tryptophan ethyl ester at pH 8.0.
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The zinc content of rhodanese.
TL;DR: It is unlikely that zinc ion can serve as the cationic site in the enzyme catalyzed cleavage of the sulfur-sulfur bond of the substrate, as zinc is absent in the fully active native enzyme and the addition of zinc ion does not enhance catalytic activity.