Yang Shen1, Ad Bax. 1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA, shenyang@niddk.nih.gov.
Abstract
Chemical shifts are obtained at the first stage of any protein structural study by NMR spectroscopy. Chemical shifts are known to be impacted by a wide range of structural factors, and the artificial neural network based TALOS-N program has been trained to extract backbone and side-chain torsion angles from (1)H, (15)N, and (13)C shifts. The program is quite robust and typically yields backbone torsion angles for more than 90 % of the residues and side-chain χ 1 rotamer information for about half of these, in addition to reliably predicting secondary structure. The use of TALOS-N is illustrated for the protein DinI, and torsion angles obtained by TALOS-N analysis from the measured chemical shifts of its backbone and (13)C(β) nuclei are compared to those seen in a prior, experimentally determined structure. The program is also particularly useful for generating torsion angle restraints, which then can be used during standard NMR protein structure calculations.
Chemical shifts are obtained at the first stage of any protein structural study by NMR spectrosn class="Chemical">copy. Chemical shifts are known to be impacted by a wide range of structural factors, and the artificial neural network based TALOS-Nprogram has been trained to extract backbone and side-chain torsion angles from (1)H, (15)N, and (13)C shifts. The program is quite robust and typically yields backbone torsion angles for more than 90 % of the residues and side-chain χ 1 rotamer information for about half of these, in addition to reliably predicting secondary structure. The use of TALOS-N is illustrated for the protein DinI, and torsion angles obtained by TALOS-N analysis from the measured chemical shifts of its backbone and (13)C(β) nuclei are compared to those seen in a prior, experimentally determined structure. The program is also particularly useful for generating torsion angle restraints, which then can be used during standard NMR protein structure calculations.
Authors: Samuel A Kotler; Vitali Tugarinov; Thomas Schmidt; Alberto Ceccon; David S Libich; Rodolfo Ghirlando; Charles D Schwieters; G Marius Clore Journal: Proc Natl Acad Sci U S A Date: 2019-02-11 Impact factor: 11.205
Authors: Shibani Bhattacharya; Christopher B Stanley; William T Heller; Peter A Friedman; Zimei Bu Journal: J Biol Chem Date: 2019-06-06 Impact factor: 5.157
Authors: Alberto Ceccon; Thomas Schmidt; Vitali Tugarinov; Samuel A Kotler; Charles D Schwieters; G Marius Clore Journal: J Am Chem Soc Date: 2018-05-14 Impact factor: 15.419