The contribution of intrinsic disorder prediction to the elucidation of protein function

Curr Opin Struct Biol. 2013 Jun;23(3):467-72. doi: 10.1016/j.sbi.2013.02.001. Epub 2013 Mar 1.

Abstract

Current knowledge of protein function stems primarily from the detailed characterization of some protein domain families and from extensive homology-based annotation transfers. Intrinsically disordered proteins exploit complementary molecular recognition mechanisms and their study has potential to make a significant contribution to the field. Building on established computational biology techniques, efforts are now aimed at unveiling their biological roles at the molecular and system level. Recent developments towards identifying functional sites in disordered regions, and analysing how the occurrence of protein disorder in a gene can provide insight into its biochemical and cellular function are discussed.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Computational Biology / methods
  • Databases, Protein
  • Humans
  • Intrinsically Disordered Proteins / chemistry*
  • Intrinsically Disordered Proteins / genetics
  • Intrinsically Disordered Proteins / metabolism*
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • Proteome
  • Sequence Analysis, Protein

Substances

  • Intrinsically Disordered Proteins
  • Proteome