Protein Frustratometer 2: a tool to localize energetic frustration in protein molecules, now with electrostatics

Nucleic Acids Res. 2016 Jul 8;44(W1):W356-60. doi: 10.1093/nar/gkw304. Epub 2016 Apr 29.

Abstract

The protein frustratometer is an energy landscape theory-inspired algorithm that aims at localizing and quantifying the energetic frustration present in protein molecules. Frustration is a useful concept for analyzing proteins' biological behavior. It compares the energy distributions of the native state with respect to structural decoys. The network of minimally frustrated interactions encompasses the folding core of the molecule. Sites of high local frustration often correlate with functional regions such as binding sites and regions involved in allosteric transitions. We present here an upgraded version of a webserver that measures local frustration. The new implementation that allows the inclusion of electrostatic energy terms, important to the interactions with nucleic acids, is significantly faster than the previous version enabling the analysis of large macromolecular complexes within a user-friendly interface. The webserver is freely available at URL: http://frustratometer.qb.fcen.uba.ar.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms*
  • Amino Acid Sequence
  • Computer Graphics
  • Humans
  • Internet
  • Molecular Dynamics Simulation
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nucleic Acids / chemistry*
  • Nucleic Acids / genetics
  • Nucleosomes / chemistry*
  • Nucleosomes / genetics
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Sequence Analysis, Protein
  • Static Electricity
  • Thermodynamics
  • User-Computer Interface*

Substances

  • Nuclear Proteins
  • Nucleic Acids
  • Nucleosomes