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Issue 54, 2019
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Rapid NMR assignments of intrinsically disordered proteins using two-dimensional 13C-detection based experiments

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Abstract

An approach for rapid backbone resonance assignments in proteins using only two 2D NMR experiments is presented. The new method involves a combination of high-resolution 13Cα-detected NMR experiments and selective unlabeling of amino acid residues. The 13C detected 2D hNCA and 2D hNcoCA spectra of a uniformly labeled sample of the protein are analysed in concert with the 2D hNCA spectrum obtained for a selectively unlabeled sample. The combinatorial set of amino acid residues for selective unlabeling is chosen optimally to maximize the assignments. The method is useful for rapid assignment of proteins with low stability such as intrinsically disordered proteins and is applicable to deuterated proteins. This approach helped in assignments of 14.5 kDa human α-synuclein during the course of its aggregation.

Graphical abstract: Rapid NMR assignments of intrinsically disordered proteins using two-dimensional 13C-detection based experiments

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Publication details

The article was received on 07 May 2019, accepted on 10 Jun 2019 and first published on 10 Jun 2019


Article type: Communication
DOI: 10.1039/C9CC03530C
Chem. Commun., 2019,55, 7820-7823

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    Rapid NMR assignments of intrinsically disordered proteins using two-dimensional 13C-detection based experiments

    S. Sukumaran, S. A. Malik, S. S. R., K. Chandra and H. S. Atreya, Chem. Commun., 2019, 55, 7820
    DOI: 10.1039/C9CC03530C

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