CoNSEnsX+ Webserver for the Analysis of Protein Structural Ensembles Reflecting Experimentally Determined Internal Dynamics

Dániel Dudola, Bertalan Kovács, Z. Gáspári

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Ensemble-based models of protein structure and dynamics reflecting experimental parameters are increasingly used to obtain deeper understanding of the role of dynamics in protein function. Such ensembles differ substantially from those routinely deposited in the PDB and, consequently, require specialized validation and analysis methodology. Here we describe our completely rewritten online validation tool, CoNSEnsX+, that offers a standardized way to assess the correspondence of such ensembles to experimental NMR parameters. The server provides a novel selection feature allowing a user-selectable set and weights of different parameters to be considered. This also offers an approximation of potential overfitting, namely, whether the number of conformers necessary to reflect experimental parameters can be reduced in the ensemble provided. The CoNSEnsX+ webserver is available at consensx.itk.ppke.hu. The corresponding Python source code is freely available on GitHub (github.com/PPKE-Bioinf/consensx.itk.ppke.hu).

Original languageEnglish
Pages (from-to)1728-1734
Number of pages7
JournalJournal of Chemical Information and Modeling
Volume57
Issue number8
DOIs
Publication statusPublished - Aug 28 2017

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Proteins
Feature extraction
Servers
Nuclear magnetic resonance
methodology

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)
  • Computer Science Applications
  • Library and Information Sciences

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CoNSEnsX+ Webserver for the Analysis of Protein Structural Ensembles Reflecting Experimentally Determined Internal Dynamics. / Dudola, Dániel; Kovács, Bertalan; Gáspári, Z.

In: Journal of Chemical Information and Modeling, Vol. 57, No. 8, 28.08.2017, p. 1728-1734.

Research output: Contribution to journalArticle

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