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Title: Spectral editing: selection of methyl groups in multidimensional solid-state magic-angle spinning NMR. Author: Jehle S, Hiller M, Rehbein K, Diehl A, Oschkinat H, van Rossum BJ. Journal: J Biomol NMR; 2006 Nov; 36(3):169-77. PubMed ID: 17031530. Abstract: A simple spectroscopic filtering technique is presented that may aid the assignment of (13)C and (15)N resonances of methyl-containing amino-acids in solid-state magic-angle spinning (MAS) NMR. A filtering block that selects methyl resonances is introduced in two-dimensional (2D) (13)C-homonuclear and (15)N-(13)C heteronuclear correlation experiments. The 2D (13)C-(13)C correlation spectra are recorded with the methyl filter implemented prior to a (13)C-(13)C mixing step. It is shown that these methyl-filtered (13)C-homonuclear correlation spectra are instrumental in the assignment of C(delta) resonances of leucines by suppression of C(gamma)-C(delta) cross peaks. Further, a methyl filter is implemented prior to a (15)N-(13)C transferred-echo double resonance (TEDOR) exchange scheme to obtain 2D (15)N-(13)C heteronuclear correlation spectra. These experiments provide correlations between methyl groups and backbone amides. Some of the observed sequential (15)N-(13)C correlations form the basis for initial sequence-specific assignments of backbone signals of the outer-membrane protein G.[Abstract] [Full Text] [Related] [New Search]