Startseite
English
Erweiterte Suche
Durchblättern nach ...
Publikationen im Überblick
Ansprechpartner
Hilfe
DOI
 |
|
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten
[➜Einloggen]
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
Zeitschrift
Journal of Biomolecular NMR
Quellenangaben
Band: 59,
Heft: 4,
Seiten: 241-249
Verlag
Springer
Verlagsort
Dordrecht
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)