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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 Ed Engl. 2016; 55(47):14847-14851 [OPEN ACCESS]
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Autor/innen der Med Uni Graz:
Madl Tobias
Viertler Martin

Dimensions Citations:

Plum Analytics:
Number of Figures: 2
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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. © 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Find related publications in this database (using NLM MeSH Indexing)
Intrinsically Disordered Proteins - chemistry
Lanthanoid Series Elements - chemistry
Magnetic Resonance Spectroscopy -

Find related publications in this database (Keywords)
chemical-shift dispersion
intrinsically disordered proteins
pseudo-contact shifts
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