Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional (1)H-detected solid-state NMR
 

Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional (1)H-detected solid-state NMR

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...

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