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Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins.
J. Biomol. NMR 59, 241-249 (2014)
Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diffusion, and can be affected by paramagnetic impurities as e.g. oxygen, which make a quantitative interpretation difficult. We present here the site-specific measurement of [1H]13C and [1H]15N heteronuclear rates in an immobilized protein. For methyls, a strong effect is expected due to the three-fold rotation of the methyl group. Quantification of the [1H]13C heteronuclear NOE in combination with 13C-R1 can yield a more accurate analysis of side chain motional parameters. The observation of significant [1H]15N heteronuclear NOEs for certain backbone amides, as well as for specific asparagine/glutamine sidechain amides is consistent with MD simulations. The measurement of site-specific heteronuclear NOEs is enabled by the use of highly deuterated microcrystalline protein samples in which spin diffusion is reduced in comparison to protonated samples.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Deuteration ; Mas Solid-state Nmr ; Protein Dynamics ; Spin Relaxation; Solid-state Nmr; Nuclear-magnetic-resonance; Side-chain Dynamics; Backbone Dynamics; Perdeuterated Proteins; Relaxation Rates; Time-scale; Molecular Simulation; Crystalline Protein; Dipolar Couplings
ISSN (print) / ISBN
0925-2738
e-ISSN
1573-5001
Journal
Journal of Biomolecular NMR
Quellenangaben
Volume: 59,
Issue: 4,
Pages: 241-249
Publisher
Springer
Publishing Place
Dordrecht
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)