NMR paper Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.

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[NMR paper] Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.

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12-15-2015, 08:09 PM

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Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.

Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.

Rapid NMR assignments of proteins using optimized combinatorial selective unlabeling.

Chembiochem. 2015 Dec 10;

Authors: Atreya HS, Dubey A, Jaipuria G, Kadumuri RV, Vadrevu R

Abstract
A new approach for rapid resonance assignments in proteins based on amino acid selective unlabeling is presented. The method involves choosing a set of multiple amino acid types for selective unlabeling and identifying specific tri-peptides surrounding the labeled residues using two-dimensional (2D) NMR spectra in a combinatorial manner. It is shown that a 2D [15N-1H] HSQC spectrum along with two 2D spectra can yield ~50% assignments directly. The methodology is applicable to deuterated proteins and was applied to two systems: an intrinsically disordered protein (12 kDa) and 29 kDa (268 residues) ?-subunit of Escherichia coli tryptophan synthase, presenting a challenging case with spectral overlaps and missing peaks. Taken together, the method can augment conventional approaches and/or will be useful for applications such as identifying active-site residues, residues involved in ligand binding or protein-protein interactions even prior to complete resonance assignments.

PMID: 26662553 [PubMed - as supplied by publisher]

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