Binding and Folding of Intrinsically Disordered Proteins: Nascent structures vs instinsic flexiblity

Abstract
Intrinsically disordered proteins (IDPs) are a class of newly recognized functional proteins that rely on a lack of stable structure for function. They are highly prevalent in biology, play key roles in crucial cellular functions, and are extensively involved human diseases. For signaling and regulation, IDPs frequently fold into stable structures upon recognition of specific targets. Understanding the mechanisms of these binding folding interactions is of significant importance because they underlie the organization of important regulatory networks that control various aspects of cellular decision-making. I will discuss some of the key lessons that we have learned from our recent atomistic and coarse-grained simulations of several small regulatory IDPs. In particular, I will discuss how an intriguing interplay of nascent structures, intrinsic flexibility, and charges might facilitate efficient and versatile regulation of IDP function. Binding and Folding of Intrinsically Disordered Proteins: Nascent structures vs instinsic flexibility, and charges might facilitate efficient and versatile regulation of IDP function.

Bio
Dr. Chen’s lab focuses both on developing novel molecular modeling methodologies and applying these techniques to study the structure, dynamics and interaction of functional proteins including intrinsically disordered proteins. He is a 2010 NSF CAREER awardee and 2011 ACS HP Outstanding Junior Faculty in Computational Chemistry.