Thread: Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMR [Biophysics and Computational Biology]
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Default Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMR [Biophysics and Computational Biology]
Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional 1H-detected solid-state NMR [Biophysics and Computational Biology]

Alexander Klein, Petra Rovo, Varun V. Sakhrani, Yangyang Wang, Jacob B. Holmes, Viktoriia Liu, Patricia Skowronek, Laura Kukuk, Suresh K. Vasa, Peter Guntert, Leonard J. Mueller, Rasmus Linser...
Date: 2022-01-20

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... Read More


PNAS:
Number: 4
Volume: 119
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