Hydrolysis of a Ni-Schiff-Base Complex Using Conditions Suitable for Retention of Acid-labile Protecting Groups
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چکیده
منابع مشابه
Study the Interaction of Ni Complex of Tetradentate Schiff Base Ligand with HEN Egg White Lysozyme
AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...
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Factors affecting aspartimide formation, such as protecting groups, acidity, basicity, and temperature, were studied using the model tetrapeptide, Glu-AspGly-Thr. The aspartyl carboxyl side chain in this tetrapeptide was either free or protected as a benzyl or cyclohexyl ester. Our results showed that the cyclohexyl ester led to far less aspartimide formation during acidic or tertiary amine tre...
متن کاملstudy the interaction of ni complex of tetradentate schiff base ligand with hen egg white lysozyme
abstractinteraction of ni complex(salen= n, n´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (hewl) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. the protein binding affinity of ni complex was found to be (3.0×103m−1). the binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 m-1. i...
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ژورنال
عنوان ژورنال: Journal of Visualized Experiments
سال: 2017
ISSN: 1940-087X
DOI: 10.3791/55677