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Protein NMR Resonance Assignment without Spectral Analysis: 5D SOlid‐State Automated Projection SpectroscopY (SO‐APSY)
Author(s) -
Orton Henry W.,
Stanek Jan,
Schubeis Tobias,
Foucaudeau Dylan,
Ollier Claire,
Draney Adrian W.,
Le Marchand Tanguy,
CalaDe Paepe Diane,
Felli Isabella C.,
Pierattelli Roberta,
Hiller Sebastian,
Bermel Wolfgang,
Pintacuda Guido
Publication year - 2020
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.201912211
Subject(s) - nuclear magnetic resonance spectroscopy , solid state nuclear magnetic resonance , projection (relational algebra) , spectroscopy , magic angle spinning , chemistry , chemical shift , analytical chemistry (journal) , nuclear magnetic resonance , coherence (philosophical gambling strategy) , computational physics , biological system , materials science , physics , computer science , algorithm , chromatography , quantum mechanics , biology
Narrow proton signals, high sensitivity, and efficient coherence transfers provided by fast magic‐angle spinning at high magnetic fields make automated projection spectroscopy feasible for the solid‐state NMR analysis of proteins. We present the first ultrahigh dimensional implementation of this approach, where 5D peak lists are reconstructed from a number of 2D projections for protein samples of different molecular sizes and aggregation states, which show limited dispersion of chemical shifts or inhomogeneous broadenings. The resulting datasets are particularly suitable to automated analysis and yield rapid and unbiased assignments of backbone resonances.