کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2188978 | 1096192 | 2006 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Macromolecular Crowding Stabilizes the Molten Globule Form of Apomyoglobin with Respect to Both Cold and Heat Unfolding
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
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چکیده انگلیسی
At pH 2 apomyoglobin is extensively unfolded. Addition of increasing concentration of salts has been shown to convert the protein into molten globule form(s), which can undergo both heat-induced and cold-induced unfolding. Increasing concentrations of an inert polymer, dextran, lead to increased formation of molten globule and stabilizes the protein with respect to both heat-induced and cold-induced denaturation. The transitions were studied by circular dichroism. Two-state analysis of the data shows that the effects of salt and polymer are additive, and that stabilization by the polymer is independent of temperature, as predicted by excluded volume theory.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 361, Issue 1, 4 August 2006, Pages 7–10
Journal: Journal of Molecular Biology - Volume 361, Issue 1, 4 August 2006, Pages 7–10
نویسندگان
Peter McPhie, Yi-sheng Ni, Allen P. Minton,