title: Evolution and disorder.
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.
authors.affiliation: Department of Biological Sciences, IBEST, University of Idaho, Moscow, ID 83844-3051, United States. celesteb@uidaho.edu
authors.forename: Celeste J
authors.initials: CJ
authors.lastname: Brown
authors.forename: Audra K
authors.initials: AK
authors.lastname: Johnson
authors.forename: A Keith
authors.initials: AK
authors.lastname: Dunker
authors.forename: Gary W
authors.initials: GW
authors.lastname: Daughdrill
mesh_terms: D000818:Animals; D020134:Catalytic Domain / Q000235:genetics; D019143:Evolution, Molecular; D006801:Humans; D017354:Point Mutation / Q000235:genetics; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: D011506:Proteins