Protein Crystallization by Anodic Porous Alumina (APA) Template: The Example of Hen Egg White Lysozyme (HEWL)
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 کاملHigh-pressure protein crystallography of hen egg-white lysozyme
Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950 MPa are presented. From 0.1 to 710 MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890 MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950 MPa, the tetragonal crystal of HEWL undergoes...
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 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 کاملCrystallization and evaluation of hen egg-white lysozyme crystals for protein pH titration in the crystalline state
To observe the ionized status of the amino acid residues in proteins at different pH (protein pH titration in the crystalline state) by neutron diffraction, hen egg-white lysozyme was crystallized over a wide pH range (2.5-8.0). Crystallization phase diagrams at pH 2.5, 6.0 and 7.5 were determined. At pH < 4.5 the border between the metastable region and the nucleation region shifted to the lef...
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ژورنال
عنوان ژورنال: NanoWorld Journal
سال: 2015
ISSN: 2379-1101
DOI: 10.17756/nwj.2015-006