Conformational Flexibility and Function in Intrinsically Disordered and Ordered Proteins
Feb 15, Wed, 2006
3:30pm - 4:30pm, 1005 Malott
Proteins are dynamic molecules and often undergo conformational change upon ligand binding. It is widely accepted that flexible loop regions have a critical functional role in enzymes. Lack of consideration of binding site flexibility has led to failures in predicting protein functions and in successfully docking ligands with protein receptors. This talk would focus on conformational flexibility and function in intrinsically disordered and ordered or stable proteins. Intrinsically disordered proteins are structured only upon binding their partner molecule. Thus, they provide an extreme example of conformational flexibility. In contrast, enzymes have well defined stable (or ordered) structures and often undergo conformational change upon ligand binding. We use bioinformatics and molecular dynamics simulations techniques to address the following questions: (i) how different are the sequence and structural features of disordered and ordered proteins, (ii) is there an evolutionary pressure for functional loop flexibility, and (iii) do sequence and structural features distinguish the structurally flexible and rigid binding sites?