Journal
STRUCTURE
Volume 21, Issue 9, Pages 1492-1499Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.08.001
Keywords
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Funding
- Canadian Institutes for Health Research
- Canadian Cancer Society Research Institute, Cystic Fibrosis Canada
- Cystic Fibrosis Foundation Therapeutics
- Natural Science and Engineering Research Council of Canada
- V. Foundation Scholar Grant, National Cancer Institute Cancer Center Support grant [P30CA21765]
- American Lebanese Syrian Associated Charities
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Intrinsically disordered proteins (IDPs), which lack persistent structure, are a challenge to structural biology due to the inapplicability of standard methods for characterization of folded proteins as well as their deviation from the dominant structure/function paradigm. Their widespread presence and involvement in biological function, however, has spurred the growing acceptance of the importance of IDPs and the development of new tools for studying their structure, dynamics, and function. The interplay of folded and disordered domains or regions for function and the existence of a continuum of protein states with respect to conformational energetics, motional timescales, and compactness are shaping a unified understanding of structure-dynamics-disorder/function relationships. In the 20th anniversary of Structure, we provide a historical perspective on the investigation of IDPs and summarize the sequence features and physical forces that underlie their unique structural, functional, and evolutionary properties.
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