4.5 Article

Evolution and disorder

期刊

CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 21, 期 3, 页码 441-446

出版社

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2011.02.005

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资金

  1. National Institutes of Health [P20RR16448, R01 LM007688, R02GM071714]
  2. National Science Foundation [0939014, MCB-0849803]
  3. American Cancer Society [RSG-07-289-01-GMC]
  4. Direct For Biological Sciences
  5. Div Of Molecular and Cellular Bioscience [939014] Funding Source: National Science Foundation
  6. Emerging Frontiers
  7. Direct For Biological Sciences [0849803] Funding Source: National Science Foundation

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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.

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