期刊
JOURNAL OF BIOMOLECULAR NMR
卷 51, 期 4, 页码 477-485出版社
SPRINGER
DOI: 10.1007/s10858-011-9578-1
关键词
Solid-state NMR; Micro-crystalline; Membrane proteins; Ubiquitin; OmpG; Deuterium-carbon correlations
资金
- Marie Cruie FP7-ITN (SBMP) [211800]
Well-resolved (2)H-(13)C correlation spectra, reminiscent of (1)H-(13)C correlations, are obtained for perdeuterated ubiquitin and for perdeuterated outer-membrane protein G (OmpG) from E. coli by exploiting the favorable lifetime of (2)H double-quantum (DQ) states. Sufficient signal-to-noise was achieved due to the short deuterium T (1), allowing for high repetition rates and enabling 3D experiments with a (2)H-(13)C transfer step in a reasonable time. Well-resolved 3D (2)H(DQ)-(13)C-(13)C correlations of ubiquitin and OmpG were recorded within 3.5 days each. An essentially complete assignment of (2)H(DQ alpha) shifts and of a substantial fraction of (2)H(DQ beta) shifts were obtained for ubiquitin. In the case of OmpG, (2)H(DQ alpha) and (2)H(DQ beta) chemical shifts of a considerable number of threonine, serine and leucine residues were assigned. This approach provides the basis for a general heteronuclear 3D MAS NMR assignment concept utilizing pulse sequences with (2)H(DQ)-(13)C transfer steps and evolution of deuterium double-quantum chemical shifts.
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