作者: Tessa Sinnige , Mark Daniëls , Marc Baldus , Markus Weingarth
DOI: 10.1021/JA412870M
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摘要: We show that selective labeling of proteins with protonated amino acids embedded in a perdeuterated matrix, dubbed 'proton clouds', provides general access to long-range contacts between nonexchangeable side chain protons proton-detected solid-state NMR, which is important study protein tertiary structure. Proton-cloud significantly improves spectral resolution by simultaneously reducing proton line width and crowding despite high local density clouds. The approach amenable almost all canonical acids. Our method demonstrated on ubiquitin the β-barrel membrane BamA.