Evolution and disorder

Celeste J. Brown, Audra K. Johnson, A. Keith Dunker, Gary W. Daughdrill

Research output: Contribution to journalReview article

154 Scopus citations

Abstract

The evolution of disordered proteins or regions of proteins differs from that of ordered proteins because of the differences in their sequence composition, intramolecular contacts, and function. Recent assessments of disordered protein evolution at the sequence, structural, and functional levels support this hypothesis. Disordered proteins have a different pattern of accepted point mutations, exhibit higher rates of insertions and deletions, and generally, but not always, evolve more rapidly than ordered proteins. Even with these high rates of sequence evolution, a few examples have shown that disordered proteins maintain their flexibility under physiological conditions, and it is hypothesized that they maintain specific structural ensembles.

Original languageEnglish (US)
Pages (from-to)441-446
Number of pages6
JournalCurrent Opinion in Structural Biology
Volume21
Issue number3
DOIs
StatePublished - Jun 1 2011

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Brown, C. J., Johnson, A. K., Dunker, A. K., & Daughdrill, G. W. (2011). Evolution and disorder. Current Opinion in Structural Biology, 21(3), 441-446. https://doi.org/10.1016/j.sbi.2011.02.005