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Lopez del Amo, J.M. ; Agarwal, V.* ; Sarkar, R. ; Porter, J. ; Asami, S. ; Rübbelke, M. ; Fink, U.* ; Xue, Y.* ; Lange, O.F. ; Reif, B.

Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins.

J. Biomol. NMR 59, 241-249 (2014)
Verlagsversion DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 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
Quellenangaben Band: 59, Heft: 4, Seiten: 241-249 Artikelnummer: , Supplement: ,
Verlag Springer
Verlagsort Dordrecht
Begutachtungsstatus Peer reviewed