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Backbone Assignment of Fully Protonated Solid Proteins by 1 H Detection and Ultrafast Magic‐Angle‐Spinning NMR Spectroscopy
Author(s) -
Marchetti Alessandro,
Jehle Stefan,
Felletti Michele,
Knight Michael J.,
Wang Yao,
Xu ZhiQiang,
Park Ah Young,
Otting Gottfried,
Lesage Anne,
Emsley Lyndon,
Dixon Nicholas E.,
Pintacuda Guido
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201203124
Subject(s) - microcrystalline , magic angle spinning , protonation , ultrashort pulse , solid state nuclear magnetic resonance , spectroscopy , nuclear magnetic resonance spectroscopy , spinning , analytical chemistry (journal) , crystallography , chemistry , magic angle , nuclear magnetic resonance spectroscopy of nucleic acids , materials science , nuclear magnetic resonance , physics , transverse relaxation optimized spectroscopy , fluorine 19 nmr , stereochemistry , optics , chromatography , organic chemistry , polymer chemistry , ion , laser , quantum mechanics
Narrow 1 H 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 1 H, 15 N, 13 C α , and 13 CO resonances and yields information about 1 H– 1 H proximities.