Structural analysis of thiol modified beta-lactoglobulin by using NMR
نویسندگان
چکیده
منابع مشابه
pH-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...
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To clarify the pH-dependent conformational transitions of proteins, we propose an approach in which structural changes monitored by heteronuclear sequential quantum correlation (HSQC) spectroscopy were analyzed by using a principal component analysis (PCA). We use bovine beta-lactoglobulin, a protein widely used in protein folding studies, as a target. First, we measured HSQC spectra at various...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s24_3