Study of the Thermal-Denaturation Mechanism of Hen Egg-White Lysozyme through Proteolytic Degradation
نویسندگان
چکیده
منابع مشابه
DMSO-induced denaturation of hen egg white lysozyme.
We report on the size, shape, structure, and interactions of lysozyme in the ternary system lysozyme/DMSO/water at low protein concentrations. Three structural regimes have been identified, which we term the "folded" (0 < φ(DMSO) < 0.7), "unfolded" (0.7 ≤ φ(DMSO) < 0.9), and "partially collapsed" (0.9 ≤ φ(DMSO) < 1.0) regime. Lysozyme resides in a folded conformation with an average radius of g...
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 کاملthermal aggregation of hen egg white lysozyme: effect of polyamines
protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutati...
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 کاملDenaturation of hen egg white lysozyme in electromagnetic fields: a molecular dynamics study.
Nonequilibrium molecular dynamics simulations of hen egg white lysozyme have been performed in the canonical ensemble at 298 K in the presence of external electromagnetic fields of varying intensity in the microwave to far-infrared frequency range. Significant nonthermal field effects were noted, such as marked changes in the protein's secondary structure which led to accelerated incipient loca...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1972
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1972.tb01786.x