کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926450 | 1536464 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Favorable contribution of the C-terminal residue K97 to the stability of a hyperthermophilic archaeal [P62A]Ssh10b
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The role of residue K97 at the C-terminal end of archaeal [P62A]Ssh10b in the hyperthermostability of the protein is investigated using three K97-mutant variants: K97E-, K97A-, and ÎK97-mutant [P62A]Ssh10b. The thermal- and GdmHCl-induced denaturation of the three mutant variants has been monitored by circular dichroism. The results reveal that the K97E mutation leads to a stronger destabilization effect than the K97A mutation by disturbing the electrostatic interaction of the salt-bridge D63-K97 and drawing an unfavorable charge-charge repulsive interaction into the structure. However, ÎK97-[P62A]Ssh10b shows much lower stability than K97E- and K97A-mutant [P62A]Ssh10b. Analysis suggests that residue K97 at the C-terminal end makes the favorable contributions to the stability of hyperthermophilic [P62A]Ssh10b not only by the favorable electrostatic interactions with residues in close vicinity but also through maintaining the side chain packing of the surrounding residues in the C-terminal area of the protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 481, Issue 1, 1 January 2009, Pages 52-58
Journal: Archives of Biochemistry and Biophysics - Volume 481, Issue 1, 1 January 2009, Pages 52-58
نویسندگان
Xianyang Fang, Yingang Feng, Jinfeng Wang,