Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 67, Issue -, Pages 219-225Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2020.12.012
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Funding
- National Institutes of Health [R01NS116176, R01GM120537, R01AG05605]
- National Science Foundation [DMR2004796, MCB-1716956, TG-MCA05S027, CNS-1725797, DMR 1720256]
- Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health
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Intrinsically disordered proteins (IDPs) are a special class of proteins that do not fold into specific 3D shapes, making experimental studies challenging and requiring theoretical and computational methods. Recent progress has been made in developing new computational and theoretical approaches to study the structure and dynamics of IDPs, particularly their phase separation into protein-rich condensates.
Intrinsically disordered proteins (IDPs) are an important class of proteins that do not fold to a well-defined three-dimensional shape but rather adopt an ensemble of inter-converting conformations. This feature makes their experimental characterization challenging and invites a theoretical and computational approach to complement experimental studies. In this review, we highlight the recent progress in developing new computational and theoretical approaches to study the structure and dynamics of monomeric and order higher assemblies of IDPs, with a particular emphasis on their phase separation into protein-rich condensates.
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