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Long‐Range Correlations between Aliphatic 13 C Nuclei in Protein MAS NMR Spectroscopy
Author(s) -
Bayro Marvin J.,
Maly Thorsten,
Birkett Neil R.,
Dobson Christopher M.,
Griffin Robert G.
Publication year - 2009
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.200901520
Subject(s) - homonuclear molecule , magic angle spinning , nuclear magnetic resonance spectroscopy , chemistry , polarization (electrochemistry) , dipole , nuclear magnetic resonance , analytical chemistry (journal) , crystallography , physics , molecule , organic chemistry
Highly efficient polarization transfer can be achieved in the magic‐angle spinning NMR analysis of proteins by the combination of 13 C labeling at alternating positions and band‐selective radio‐frequency‐driven recoupling (BASE RFDR), a pulse scheme aimed at exploiting the bandwidth selectivity and favorable effects of weak 13 C radio‐frequency irradiation to reintroduce the homonuclear dipolar interactions between distant nuclei.