Agarwal Vipin, Faelber Katja, Schmieder Peter, Reif Bernd
Leibniz-Institut fur Molekulare Pharmakologie (FMP), Robert-Rossle-Strasse 10, 13125 Berlin, Germany.
J Am Chem Soc. 2009 Jan 14;131(1):2-3. doi: 10.1021/ja803620r.
We show in this manuscript that (2)H,(13)C correlation spectra in uniformly (2)H,(13)C isotopically enriched peptides and proteins can be recorded in MAS solid-state NMR with site specific resolution. A resolved deuterium dimension is obtained by evolving (2)H double-quantum coherences. Experimental (2)H line widths are obtained that are as small as 16 Hz (0.17 ppm at 600 MHz) in the double-quantum dimension. The unprecedented resolution in the deuterium dimension obtained for proteins opens new perspectives for correlation experiments and, in particular, for the characterization of dynamics of proteins in the solid-state.
我们在本论文中表明，在均匀（2）H、（13）C同位素富集的肽和蛋白质中，（2）H、（13）C相关谱可以在具有位点特异性分辨率的MAS固态核磁共振中记录。通过演化（2）H双量子相干获得解析的氘维度。在双量子维度中获得的实验（2）H线宽小至16 Hz（600 MHz时为0.17 ppm）。蛋白质在氘维度中获得的前所未有的分辨率为相关实验，特别是为固态蛋白质动力学的表征开辟了新的前景。
