کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048401 | 1074079 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase Kinetic and thermodynamic properties of the folding and assembly of formate dehydrogenase](/preview/png/2048401.png)
چکیده انگلیسی
The folding mechanism and stability of dimeric formate dehydrogenase from Candida methylica was analysed by exposure to denaturing agents and to heat. Equilibrium denaturation data yielded a dissociation constant of about 10−13 M for assembly of the protein from unfolded chains and the kinetics of refolding and unfolding revealed that the overall process comprises two steps. In the first step a marginally stable folded monomeric state is formed at a rate (k1) of about 2 × 10−3 s−1 (by deduction k−1 is about10−4 s−1) and assembles into the active dimeric state with a bimolecular rate constant (k2) of about 2 × 104 M−1 s−1. The rate of dissociation of the dimeric state in physiological conditions is extremely slow (k−2 ∼ 3 × 10−7 s−1).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 583, Issue 17, 3 September 2009, Pages 2887–2892
Journal: FEBS Letters - Volume 583, Issue 17, 3 September 2009, Pages 2887–2892
نویسندگان
Emel B. Ordu, Gus Cameron, Anthony R. Clarke, Nevin Gül Karagüler,