Proteomic analysis and prediction of amino acid variations that influence protein posttranslational modifications

Brief Bioinform. 2019 Sep 27;20(5):1597-1606. doi: 10.1093/bib/bby036.

Abstract

Accumulative studies have indicated that amino acid variations through changing the type of residues of the target sites or key flanking residues could directly or indirectly influence protein posttranslational modifications (PTMs) and bring about a detrimental effect on protein function. Computational mutation analysis can greatly narrow down the efforts on experimental work. To increase the utilization of current computational resources, we first provide an overview of computational prediction of amino acid variations that influence protein PTMs and their functional analysis. We also discuss the challenges that are faced while developing novel in silico approaches in the future. The development of better methods for mutation analysis-related protein PTMs will help to facilitate the development of personalized precision medicine.

Keywords: amino acid variations; computational mutation analysis; network biology; posttranslational modifications; protein PTM predictor.

Publication types

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

MeSH terms

  • Amino Acid Substitution
  • Amino Acids / metabolism*
  • Computational Biology
  • Humans
  • Mutation
  • Protein Processing, Post-Translational*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Proteomics*

Substances

  • Amino Acids
  • Proteins