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Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning
Author(s) -
Jaudzems Kristaps,
Bertarello Andrea,
Chaudhari Sachin R.,
Pica Andrea,
CalaDe Paepe Diane,
BarbetMassin Emeline,
Pell Andrew J.,
Akopjana Inara,
Kotelovica Svetlana,
Gajan David,
Ouari Olivier,
Tars Kaspars,
Pintacuda Guido,
Lesage Anne
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201801016
Subject(s) - nuclear magnetic resonance spectroscopy , magic angle spinning , nmr spectra database , spectral line , spectroscopy , spinning , chemistry , paramagnetism , nuclear magnetic resonance , analytical chemistry (journal) , materials science , physics , condensed matter physics , quantum mechanics , astronomy , chromatography , polymer chemistry
Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High‐quality DNP‐enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800 MHz) and fast MAS (40 kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar‐based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long‐range contacts, which are not observed at room temperature, opening new possibilities for structure determination.