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Default Backbone NMR assignments of a topologically knotted protein in urea-denatured state.

Backbone NMR assignments of a topologically knotted protein in urea-denatured state.

Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.

Biomol NMR Assign. 2013 Jul 3;

Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST

Abstract
YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent studies on the knotted protein folding pathways using YbeA have suggested that the protein knot remains present under chemically denaturing conditions. Here, we report (1)H, (13)C and (15)N chemical shift assignments for urea-denatured YbeA, which will serve as the basis for further structural characterisations using solution state NMR spectroscopy with paramagnetic spin labeled and partial alignment media.


PMID: 23821130 [PubMed - as supplied by publisher]



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