کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
691995 | 1460463 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural bioinformatics analysis of free cysteines in protein environments
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
تکنولوژی و شیمی فرآیندی
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چکیده انگلیسی
Cysteine has been considered as a “hydrophilic” amino acid because of its pKa and its ability to form (weak) hydrogen bonds. However, cysteines are found mostly in hydrophobic environments, either in S-S (disulphide) form or in free cysteine form. When free cysteines are found on the surface of proteins, they are often involved in catalytic residues, as in cysteine proteases, P-loop phosphatases, etc. Additionally, a unique property of cysteines is that their side-chain volume is different from all other amino acids. This study is focused on the discrimination between structural versus active free cysteines based on a local environment analysis which does not appear to have been attempted previously. We have demonstrated the corresponding structural positions associated with free cysteines in their three-dimensional localization environment. We examined protein samples including nine, sequenced, coronavirus proteases and cysteine-rich non-membrane proteins. Our present study shows that the sequential environments of free cysteines of coronavirus proteases are rather hydrophobic and that the free cysteines of non-membrane proteases have a higher amount of contacts to hydrophobic residues and lower amount of contacts to polar or charged residues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of the Taiwan Institute of Chemical Engineers - Volume 40, Issue 2, March 2009, Pages 123-129
Journal: Journal of the Taiwan Institute of Chemical Engineers - Volume 40, Issue 2, March 2009, Pages 123-129
نویسندگان
Sheau Ling Ho, Andrew H.-J. Wang,