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Increasing the chemical-shift dispersion of unstructured proteins with a covalent lanthanide shift reagent.
Angew. Chem.-Int. Edit. 55, 14847-14851 (2016)
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.
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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
Zeitschrift
Angewandte Chemie - Internationale Edition
Quellenangaben
Band: 55,
Heft: 47,
Seiten: 14847-14851
Verlag
Wiley
Verlagsort
Weinheim
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)