|
|||||
|
|
Evolution and disorder |
|
| Authors: | Brown Celeste J Johnson Audra K Dunker A Keith Daughdrill Gary W |
| Institution: | 1 Department of Biological Sciences, IBEST, University of Idaho, Moscow, ID 83844-3051, United States 2 Center for Computational Biology & Bioinformatics, Biochemistry and Molecular Biology, Indiana University Schools of Medicine & Informatics, 410 W. 10th Street, Suite 5000, Indianapolis, IN 46202, United States 3 Department of Cell Biology, Microbiology and Molecular Biology, Center for Drug Discovery and Innovation, 3720 Spectrum Blvd. Suite 321, University of South Florida, Tampa, FL 33612, United States |
| 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. |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ | |