کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10429225 909700 2005 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characteristics of Two Intermediates Trapped in the Unfolding Pathway of Arginine Kinase Induced by Guanidinium Chloride
موضوعات مرتبط
مهندسی و علوم پایه سایر رشته های مهندسی مهندسی (عمومی)
پیش نمایش صفحه اول مقاله
Characteristics of Two Intermediates Trapped in the Unfolding Pathway of Arginine Kinase Induced by Guanidinium Chloride
چکیده انگلیسی
Equilibrium guanidinium chloride (GdmCl)-induced unfolding of arginine kinase (AK) was investigated by enzymatic activity, intrinsic fluorescence, 8-anilinonaphthalene-1-sulfonic acid (ANS) fluorescence, circular dichroism (CD) spectrum, and size-exclusion chromatography. The measurements showed that AK unfolded through two equilibrium intermediates: the molten globule state and the partly folded state. Both intermediates have no enzyme activity. The molten globule state exists at 0.4-0.8 mol/L GdmCl, perhaps after the N-terminal domain has unfolded but the C-terminal domain is still intact. The partly folded state occurs at 1.1-1.5 mol/L GdmCl with a hydrodynamic volume no more than 1.6-fold larger than the native state and a pronounced far UV-CD signal. Its ANS fluorescence intensity is about 50% of the molten globule state. This partly folded state shares similarities with the “burst” kinetic intermediate of protein folding.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Tsinghua Science & Technology - Volume 10, Issue 4, August 2005, Pages 461-468
نویسندگان
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