Ontology highlight
ABSTRACT:
SUBMITTER: Barbet-Massin E
PROVIDER: S-EPMC4156866 | biostudies-other | 2014 Sep
REPOSITORIES: biostudies-other
Barbet-Massin Emeline E Pell Andrew J AJ Retel Joren S JS Andreas Loren B LB Jaudzems Kristaps K Franks W Trent WT Nieuwkoop Andrew J AJ Hiller Matthias M Higman Victoria V Guerry Paul P Bertarello Andrea A Knight Michael J MJ Felletti Michele M Le Marchand Tanguy T Kotelovica Svetlana S Akopjana Inara I Tars Kaspars K Stoppini Monica M Bellotti Vittorio V Bolognesi Martino M Ricagno Stefano S Chou James J JJ Griffin Robert G RG Oschkinat Hartmut H Lesage Anne A Emsley Lyndon L Herrmann Torsten T Pintacuda Guido G
Journal of the American Chemical Society 20140818 35
Using a set of six (1)H-detected triple-resonance NMR experiments, we establish a method for sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectra of 5-30 kDa proteins. The approach relies on perdeuteration, amide (2)H/(1)H exchange, high magnetic fields, and high-spinning frequencies (ωr/2π ≥ 60 kHz) and yields high-quality NMR data, enabling the use of automated analysis. The method is validated with five examples of proteins in ...[more]