Long-Range Correlations between Aliphatic [superscript 13]C Nucleic in Protein MAS NMR Spectroscopy

Author(s)
Bayro, Marvin J.; Maly, Thorsten; Birkett, Neil R.; Dobson, Christopher M.; Griffin, Robert Guy
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Alternative title
Long-Range Correlations between Aliphatic 13C Nuclei in Protein MAS NMR Spectroscopy†
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Abstract
Highly efficient polarization transfer can be achieved in the magic-angle spinning NMR analysis of proteins by the combination of [superscript 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 [superscript 13]C radio-frequency irradiation to reintroduce the homonuclear dipolar interactions between distant nuclei.
Date issued
2009-06
URI
http://hdl.handle.net/1721.1/82060
Department
Massachusetts Institute of Technology. Department of Chemistry; Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
Journal
Angewandte Chemie International Edition
Publisher
Wiley Blackwell
Citation
Bayro, Marvin J., Thorsten Maly, Neil R. Birkett, Christopher M. Dobson, and Robert G. Griffin. “Long-Range Correlations between Aliphatic 13C Nuclei in Protein MAS NMR Spectroscopy.” Angewandte Chemie International Edition 48, no. 31 (July 20, 2009): 5708-5710.
Version: Author's final manuscript
ISSN
14337851
15213773
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