1H-NMR study on the chitotrisaccharide binding to hen egg white lysozyme
نویسندگان
چکیده
منابع مشابه
Hen 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...
متن کاملX-ray crystallographic study of binding of cobalt ion to hen egg-white lysozyme.
The present studies were carried out essentially as described by Moult et al. [3]. Tetragonal crystals of hen egg-white lysozyme [4] were grown at pH 4.7 in 0.02 M acetate buffer, containing 5% NaCl (w/v). Individual crystals (space group P4s2r2, a=b=79.1 A, C= 37.9 A) about 0.6 mm in the longest dimension, were transferred to 1 .O mm diameter quartz capillaries containing 0.1 ml mother liquor....
متن کاملStudy of protein binding sites on the GTPase RalA and the sugar - binding protein hen egg white lysozyme
Nicely, Nathan. Study of protein binding sites on the GTPase RalA and the sugar-binding protein hen egg white lysozyme. (Under the direction of Carla Mattos.) Hen egg white lysozyme and simian RalA are two very different proteins by function and category. Lysozyme is an extracellular enzyme that catalyzes the hydrolysis of the β-linkage between N-acetylmuramic acid (NAM) and N-acetylglucosamine...
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 کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1992
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1992.tb17428.x