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. Implicit solvent arguably provides an optimal balance between efficiency and accuracy necessary for modeling IDPs. I will discuss some ofl key lessons that we have learned from our recent atomistic simulations several small regulatory IDPs, particularly, how an intriguing interplay of nascent structures, conformational flexibility, and charges might facilitate efficient and versatile regulation of IDP function.

Implicit solvent simulations of intrinsically disordered proteins: Induced folding vs. conformational selection

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.