Structural Characterization of the Complex between Hen Egg-White Lysozyme and ZrIV-Substituted Keggin Polyoxometalate as Artificial Protease
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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...
متن کاملCharacterization of the unfolding pathway of hen egg white lysozyme.
After the recent discovery of a ribonuclease A unfolding intermediate [Kiefhaber, T., et al. (1995) Nature 375, 513-515], we investigated the unfolding pathway of hen egg white lysozyme. At pH* 4.00 with D2O at 10 degrees C and 6 M guanidinium chloride, unfolding shows a single, slow kinetic phase, with a relaxation time of 3300 s when monitored by circular dichroism (CD). Exchange of the trypt...
متن کاملHen Egg - white Lysozyme Crystals
Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...
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...
متن کاملRefinement of triclinic hen egg-white lysozyme at atomic resolution.
X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic crystals of hen egg-white lysozyme to 0.925 and 0.950 A resolution, respectively, using synchrotron radiation. Data from one crystal were sufficient for the low-temperature study, whereas three crystals were required at room temperature. Refinement was carried out using the programs PROLSQ, ARP an...
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ژورنال
عنوان ژورنال: Chemistry - A European Journal
سال: 2015
ISSN: 0947-6539
DOI: 10.1002/chem.201501998