کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5407205 | 1393207 | 2008 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Proton-detected scalar coupling based assignment strategies in MAS solid-state NMR spectroscopy applied to perdeuterated proteins
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Assignment of proteins in MAS (magic angle spinning) solid-state NMR relies so far on correlations among heteronuclei. This strategy is based on well dispersed resonances in the 15N dimension. In many complex cases like membrane proteins or amyloid fibrils, an additional frequency dimension is desirable in order to spread the amide resonances. We show here that proton detected HNCO, HNCA, and HNCACB type experiments can successfully be implemented in the solid-state. Coherences are sufficiently long lived to allow pulse schemes of a duration greater than 70 ms before incrementation of the first indirect dimension. The achieved resolution is comparable to the resolution obtained in solution-state NMR experiments. We demonstrate the experiments using a triply labeled sample of the SH3 domain of chicken α-spectrin, which was re-crystallized in H2O/D2O using a ratio of 1/9. We employ paramagnetic relaxation enhancement (PRE) using EDTA chelated CuII to enable rapid data acquisition.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Magnetic Resonance - Volume 193, Issue 1, July 2008, Pages 89-93
Journal: Journal of Magnetic Resonance - Volume 193, Issue 1, July 2008, Pages 89-93
نویسندگان
Rasmus Linser, Uwe Fink, Bernd Reif,