Protein complex analysis: From raw protein lists to protein interaction networks

Mass Spectrom Rev. 2017 Sep;36(5):600-614. doi: 10.1002/mas.21485. Epub 2015 Dec 28.

Abstract

The elucidation of molecular interaction networks is one of the pivotal challenges in the study of biology. Affinity purification-mass spectrometry and other co-complex methods have become widely employed experimental techniques to identify protein complexes. These techniques typically suffer from a high number of false negatives and false positive contaminants due to technical shortcomings and purification biases. To support a diverse range of experimental designs and approaches, a large number of computational methods have been proposed to filter, infer and validate protein interaction networks from experimental pull-down MS data. Nevertheless, this expansion of available methods complicates the selection of the most optimal ones to support systems biology-driven knowledge extraction. In this review, we give an overview of the most commonly used computational methods to process and interpret co-complex results, and we discuss the issues and unsolved problems that still exist within the field. © 2015 Wiley Periodicals, Inc. Mass Spec Rev 36:600-614, 2017.

Keywords: bioinformatics; co-complex purification; protein-protein interaction networks.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cluster Analysis
  • Computational Biology / methods*
  • Databases, Protein
  • Multiprotein Complexes / analysis
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / metabolism
  • Protein Interaction Mapping / methods*
  • Protein Interaction Mapping / standards
  • Protein Interaction Maps*
  • Proteins / analysis*
  • Proteins / chemistry
  • Proteins / metabolism
  • Quality Control
  • Reproducibility of Results
  • Workflow

Substances

  • Multiprotein Complexes
  • Proteins