Biophysics and Proteome Level Investigations of the Functions of Intrinsically Disordered Proteins
Our research is focused on the study of intrinsically disordered proteins. We develop and use state-of-the-art computational methods and combine these with experimental techniques to understand how information encoded in amino acid sequences of intrinsically disordered proteins governs their molecular function, contributes to organization of protein interaction networks, controls cellular decisions, and modulates the mechanisms of protein self-assembly.
Relevant diseases: Huntington's disease; Alzheimer's Disease; Prions; Cancers
Proteins or protein classes of interest: Huntingtin; Polyglutamine containing Proteins; Tau; Amyloid Beta; BHLH and BZIP Transcription Factors; Scaffolding Proteins; Nuclear Proteomes
Processes of Interest: Self-Assembly via homotypic interactions; Phase Transitions of multi-macromolecular systems; Functions via entropic machines; Proteostasis; Nuclear Transport; Prion-like propagation of aggregates
Techniques used: Atomistic and mesoscopic computer simulations; Polymer physics theories; Modeling hierarchical networks; Bioinformatics; In vitro biophysical experiments
Funding: We currently receive funding from the National Science Foundation (NSF), the National Institute for Neuronal Disorders and Stroke (NIH-NINDS), the National Institute of General Medical Sciences (NIH-NIGMS) and Washington University's Center for Biological Systems Engineering.
Last updated July 20th 2014