کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8334176 1540271 2012 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Differing structural characteristics of molten globule intermediate of peanut lectin in urea and guanidine-HCl
چکیده انگلیسی
The structural characteristics of exclusive equilibrium molten globule-like intermediate formed during peanut lectin unfolding in urea and guanidine hydrochloride (GdnHCl) have been investigated by size-exclusion chromatography, circular dichroism, fluorescence, phosphorescence, and chemical modification. The elution behavior and 8-anilino-1-naphthalenesulfonate binding indicate a less compact tertiary structure in urea than in GdnHCl. Further, the urea-induced intermediate reveals perturbed, nonnative typical β-sheet conformation in contrast to native-like atypical β-structure in GdnHCl. N-bromosuccinimide oxidation shows that none of three tryptophan residues is modified for GdnHCl-induced intermediate while one gets oxidized in urea. Such difference in tryptophan environment is supported by acrylamide quenching (Stern-Volmer constant being 3.2 and 5.8 M−1 respectively), and phosphorescence studies at 77 K which show a blue-shift of (0, 0) band from 412.4 nm (GdnHCl) to 411.4 nm (urea). These results may provide important insight into the differential effects of GdnHCl and urea on the structural characteristics of intermediate state(s) in protein folding.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 51, Issue 3, October 2012, Pages 188-195
نویسندگان
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