Intrinsically disordered proteins (IDPs) are a newly recognized class of functional proteins that rely on a lack of stable structure for function. They are highly prevalent in biology, play fundamental roles, and are extensively involved in human diseases. For signaling and regulation, IDPs often fold into stable structures upon binding to specific targets. The mechanisms of these coupled binding and folding processes are of significant importance because they underlie the organization of regulatory networks that dictate various aspects of cellular decision-making. This review first discusses the challenge in detailed experimental characterization of these heterogeneous and dynamics proteins and the unique and exciting opportunity for physics-based modeling to make crucial contributions, and then summarizes key lessons from recent de novo simulations of the structure and interactions of several regulatory IDPs.
Intrinsically Disordered Proteins in a Physics-Based World
T. Click,Debabani Ganguly,Jianhan Chen
Published 2010 in International Journal of Molecular Sciences
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- Publication year
2010
- Venue
International Journal of Molecular Sciences
- Publication date
2010-12-21
- Fields of study
Biology, Medicine, Physics
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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