Marchetti, AlessandroJehle, StefanFelletti, MicheleKnight, Michael J.Wang, YaoXu, Zhi-QiangPark, Ah YoungLesage, AnneEmsley, LyndonDixon, Nicholas EdwardPintacuda, GuidoOtting, Gottfried2015-12-071433-7851http://hdl.handle.net/1885/22428Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities.Keywords: Deuterations; DNA polymerase; Magic-angle-spinning NMR; Noncrystalline proteins; Protein samples; Protein structures; Protonated; scalar transfers; Solid protein; Ultra-fast; Deuterium; Nuclear magnetic resonance spectroscopy; Proteins; Protonation; Magic DNA polymerase; magic-angle spinning; NMR spectroscopy; protein structures; scalar transfersBackbone assignment of fully protonated solid proteins by 1 H detection and ultrafast magic-angle-spinning NMR spectroscopy201210.1002/anie.2012031242016-02-24