Long‐Range Correlations between Aliphatic  13 C Nuclei in Protein MAS NMR Spectroscopy | Zendy

Bayro Marvin J. | Zendy; Maly Thorsten | Zendy; Birkett Neil R. | Zendy; Dobson Christopher M. | Zendy; Griffin Robert G. | Zendy

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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.

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