Title: Understanding Motions Underlying Protein-Protein Binding via NMR

Abstract: Protein-protein interactions within signal transduction networks are often mediated by small, portable domains known as binding modules. The binding interfaces typically involve mobile regions of such modules. Hence, understanding the strengths and specificities of these protein-protein interactions demands an understanding of how modular mobility influences binding. Nuclear spin relaxation measurements using multi-dimensional NMR enables a residue-by-residue description of such motions on both fast and slow time scales. As such, these measurements provide a powerful approach for defining flexibility-activity relationships in binding modules. We will discuss examples in our work on WW domains.