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• W4206731227 abstract "NMR chemical shifts provide detailed information on the chemical properties of molecules, thereby complementing structural data from techniques like X-ray crystallography and electron microscopy. Detailed analysis of protein NMR data, however, often hinges on comprehensive, site-specific assignment of backbone resonances, which becomes a bottleneck for molecular weights beyond 40 to 45 kDa. Here, we show that assignments for the (2x)72-kDa protein tryptophan synthase (665 amino acids per asymmetric unit) can be achieved via higher-dimensional, proton-detected, solid-state NMR using a single, 1-mg, uniformly labeled, microcrystalline sample. This framework grants access to atom-specific characterization of chemical properties and relaxation for the backbone and side chains, including those residues important for the catalytic turnover. Combined with first-principles calculations, the chemical shifts in the β-subunit active site suggest a connection between active-site chemistry, the electrostatic environment, and catalytically important dynamics of the portal to the β-subunit from solution." @default.
• W4206731227 created "2022-01-25" @default.
• W4206731227 creator A5005166162 @default.
• W4206731227 creator A5005580682 @default.
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• W4206731227 creator A5012122374 @default.
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• W4206731227 creator A5056296491 @default.
• W4206731227 creator A5059078778 @default.
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• W4206731227 creator A5087617687 @default.
• W4206731227 creator A5091195461 @default.
• W4206731227 date "2022-01-20" @default.
• W4206731227 modified "2023-10-03" @default.
• W4206731227 title "Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional ¹ H-detected solid-state NMR" @default.
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