کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1987717 | 1540309 | 2008 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Evidence that the amino acid residue P272 of arginine kinase is involved in its activity, structure and stability
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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
In this research, the role of amino acid residue P272 of arginine kinase (AK) was investigated by site-directed mutagenesis. When the structure of AK was impaired by mutation, AK was in a partially unfolded state with more hydrophobic exposure, which was prone to aggregate under environmental stresses. Mutation at this position influences transition from the molten globule intermediate to the native state in folding process. The results provided herein may suggest that some residues near the active site may play a relatively important role in keeping AK activity and structural stability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 43, Issue 4, 1 November 2008, Pages 367–372
Journal: International Journal of Biological Macromolecules - Volume 43, Issue 4, 1 November 2008, Pages 367–372
نویسندگان
Qing-Yun Wu, Feng Li, Xiao-Yun Wang,