Intrinsically Disordered Proteins in a Physics-Based World

International Journal of Molecular Sciences

Timothy H. Click¹  Debabani Ganguly¹ 

关键词: conformational selection;    generalized Born;    implicit solvent;    induced folding;    molecular dynamics;    p21;    p27;    p53;    pKID;    replica exchange;   

DOI  :  10.3390/ijms11125292

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2010 by the authors; licensee MDPI, Basel, Switzerland.