کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1927614 | 1536531 | 2006 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Loosely packed papain prosegment displays inhibitory activity
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Most protease prosegments are co-synthesized at the N-termini of cysteine proteases and are involved in folding assistance, inhibition, and activation of their mature enzymes. By using circular dichroism, UV-difference and fluorescence spectroscopies, we studied the thermal unfolding of papain prosegment. The transition seems to be two-state and reversible, with an unfolded state prone to aggregation. Unfolding thermodynamic parameters obtained show low values both for ÎHTm and ÎCpU, indicative of a loosely packed three-dimensional conformation for the prosegment at near-neutral pH conditions. In spite of these results, fluorescence experiments demonstrate that papain prosegment is able to recognize and inhibit its cognate protease. An acid medium induces a molten globule-like state without intermediates, which in turn undergoes an irreversible thermal unfolding. Our results suggest that papain prosegment has a high degree of conformational flexibility, with the ability to form not only a molten globule-like structure in activating conditions, but also requiring an induced fit in order to be functional as inhibitor.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 446, Issue 2, 15 February 2006, Pages 151-160
Journal: Archives of Biochemistry and Biophysics - Volume 446, Issue 2, 15 February 2006, Pages 151-160
نویسندگان
Luis H. Gutiérrez-González, Arturo Rojo-DomÃnguez, Nallely E. Cabrera-González, Ruy Pérez-Montfort, A. Jaqueline Padilla-Zúñiga,