Protein structural information derived from NMR chemical shift with the neural network program TALOS-N

Methods Mol Biol. 2015:1260:17-32. doi: 10.1007/978-1-4939-2239-0_2.

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.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Carbon Isotopes / chemistry
  • Models, Molecular
  • Neural Networks, Computer*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Proteins / chemistry*
  • Proteomics / methods*
  • Software

Substances

  • Carbon Isotopes
  • Proteins