Structural characterization of the cold-denatured state of beta-lactoglobulin
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چکیده
منابع مشابه
Chloride-ion concentration dependence of molecular dimension in the acid-denatured state of equine [beta]-lactoglobulin
The chloride-ion concentration dependence of the molecular dimension in the acid-denatured state of equine -lactoglobulin (ELG) was investigated by smallangle X-ray scattering. In the presence of chloride ion, ELG has a globular and compact conformation (the A state). The molecular dimension of ELG increases little with decreasing chloride-ion concentration. A remarkable dependence was observed...
متن کاملpH-induced structural transitions in beta-lactoglobulin.
Pharmaceutique units/mg; Novo, Copenhagen, Denmark) and a-chymotrypsin (Choay, Paris, France) were, under appropriate conditions, added to the partially purified enzyme in final concentrations of 50 and 250 pg/ml and incubated at 37°C for different time intervals, ranging from 1 to 24 h. In all proteinase-treated preparations the DPP IV activity measured exceeded 90% of the original DPP IV acti...
متن کاملThe cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9.
A point mutation of a small globular protein, the C-terminal domain of L9 destabilizes the protein and leads to observable cold-denaturation at temperatures above zero. The cold denatured state is in slow exchange with the native state on the NMR time scale, and this allows the hydrodynamic properties of the cold unfolded state and the native state to be measured under identical conditions usin...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s162_3