Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 3, Pages 1094-1100Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja509367q
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Funding
- Helmholtz-Gemeinschaft
- Deutsche Forschungsgemeinschaft [Re1435, SFB1035]
- Bio-NMR project (European Commission) [261863/BIO-NMR-00010, BIO-NMR-00070]
- Center for Integrated Protein Science Munich (CIPS-M)
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We introduce a labeling scheme for magic angle spinning (MAS) solid-state NMR that is based on deuteration in combination with dilution of the carbon spin system. The labeling strategy achieves spectral editing by simplification of the H alpha C alpha and aliphatic side chain spectral region. A reduction in both proton and carbon spin density in combination with fast spinning (>= 50 kHz) is essential to retrieve artifact-free 13C-R1 relaxation data for aliphatic carbons. We obtain good agreement between the NMR experimental data and order parameters extracted from a molecular dynamics (MD) trajectory, which indicates that carbon based relaxation parameters can yield complementary information on protein backbone as well as side chain dynamics.
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