کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9587501 | 1393246 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Side-chain H and C resonance assignment in protonated/partially deuterated proteins using an improved 3D13C-detected HCC-TOCSY
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
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چکیده انگلیسی
We propose the use of 13C-detected 3D HCC-TOCSY experiments for assignment of 1H and 13C resonances in protonated and partially deuterated proteins. The experiments extend 2D C-13-start and C-13-observe TOCSY type experiments proposed earlier [J. Biomol. NMR 26 (2) (2003) 167]. Introduction of the third 1H dimension to 2D TOCSY: (i) reduces the peak overlap and (ii) increases the sensitivity per unit time, even for highly deuterated (>85%) protein samples, which makes this improved method an attractive tool for the side-chain H and C assignment of average sized proteins with natural isotope abundance as well as large partially deuterated proteins. The experiments are demonstrated with a 16Â kDa 15N, 13C-labeled non-deuterated apo-CcmE and a 48Â kDa uniformly 15N,13C-labeled and fractionally (â¼90%) deuterated dimeric sFkpA. It is predicted that this method should be suitable for the assignment of methyl 13C and 1H chemical shifts of methyl protonated, highly deuterated and 13C-labeled proteins with even higher molecular weight.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Magnetic Resonance - Volume 174, Issue 2, June 2005, Pages 200-208
Journal: Journal of Magnetic Resonance - Volume 174, Issue 2, June 2005, Pages 200-208
نویسندگان
Kaifeng Hu, Beat Vögeli, Konstantin Pervushin,