کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5370777 1503913 2015 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Native state dynamics affects the folding transition of porcine pancreatic phospholipase A2
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Native state dynamics affects the folding transition of porcine pancreatic phospholipase A2
چکیده انگلیسی


- Equilibrium unfolding of porcine pancreatic phospholipase A2 was monitored using multiple approaches.
- An unusually broad unfolding transition at remarkably high denaturant concentration was observed.
- Accompanied by exclusion of others, pronounced native state dynamics were identified as reason.

Porcine pancreatic phospholipase A2, a small and disulfide rich protein, is extremely resistant against chemically or thermally induced unfolding. Despite this marked resistance, the protein displays broad unfolding transitions resulting in comparatively low apparent thermodynamic stability. Broad unfolding transitions may result from undetected folding intermediates, residual structures in the unfolded state or an inhomogeneity of the native state. Using circular dichroism, fluorescence, and NMR spectroscopy, we ruled out the existence of stably populated folding intermediates, whereas UV absorbance measurements hinted at stable residual structures in the unfolded state. These residual structures proved, however, to have no impact on the folding parameters. Studies by limited proteolysis, CD, and NMR spectroscopy under non-denaturing conditions suggested pronounced dynamics of the protein in the native state, which as long as unrestrained by acidic pH or bound Ca2 + ions exert considerable influence on the unfolding transition.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biophysical Chemistry - Volume 206, November 2015, Pages 12-21
نویسندگان
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