PuSH - Publikationsserver des Helmholtz Zentrums München

Göbl, C. ; Resch, M. ; Strickland, M.* ; Hartlmüller, C. ; Viertler, M. ; Tjandra, N.* ; Madl, T.

Increasing the chemical-shift dispersion of unstructured proteins with a covalent lanthanide shift reagent.

Angew. Chem.-Int. Edit. 55, 14847-14851 (2016)
Verlagsversion DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The study of intrinsically disordered proteins (IDPs) by NMR often suffers from highly overlapped resonances that prevent unambiguous chemical-shift assignments, and data analysis that relies on well-separated resonances. We present a covalent paramagnetic lanthanide-binding tag (LBT) for increasing the chemical-shift dispersion and facilitating the chemical-shift assignment of challenging, repeat-containing IDPs. Linkage of the DOTA-based LBT to a cysteine residue induces pseudo-contact shifts (PCS) for resonances more than 20 residues from the spin-labeling site. This leads to increased chemical-shift dispersion and decreased signal overlap, thereby greatly facilitating chemical-shift assignment. This approach is applicable to IDPs of varying sizes and complexity, and is particularly helpful for repeat-containing IDPs and low-complexity regions. This results in improved efficiency for IDP analysis and binding studies.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Nmr ; Chemical-shift Dispersion ; Intrinsically Disordered Proteins ; Lanthanides ; Pseudo-contact Shifts; Intrinsically Disordered Proteins; Backbone Resonance Assignment; Nmr-spectroscopy; Unfolded Proteins; Biomolecular Nmr; Low-complexity; Regions; Binding; Fus; Transportin
ISSN (print) / ISBN 1433-7851
e-ISSN 1521-3773
Quellenangaben Band: 55, Heft: 47, Seiten: 14847-14851 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Begutachtungsstatus Peer reviewed