Professor Matt Bush

Professor Matt Bush
Department of Chemistry
University of Washington
Abstract

Pushing the Boundaries of Mass Spectrometry: New Tools for Protein Structure and Stability

Proteostasis is the complex network of cellular processes that maintain the proper balance, folding, and function of proteins within cells. This seminar will focus on advanced mass spectrometry (MS) technologies that we have developed for characterizing many processes that are of critical importance to proteostasis, including the folding, misfolding, degradation, and aggregation of proteins. These technologies make use of a variety of MS-based strategies, including native MS, ion mobility MS, and structural proteomics. I’ll also discuss the implications of these technologies for understanding biological processes related to aging and disease and for developing therapeutics for challenging protein targets.

Matt Bush

Professor Matt Bush pursued his PhD with Evan Williams and Richard Saykally at the University of California, Berkeley. During that time, he used IR laser spectroscopy and FT-ICR mass spectrometry (MS) to investigate zwitterion formation and ion solvation. This training in high-performance MS and physical chemistry laid the groundwork for his continued pursuits using gas-phase techniques to investigate the structures and interactions of biomolecules. He then joined the laboratory of Carol Robinson FRS DBE at the University of Cambridge and the University of Oxford, during which time he used ion mobility MS to characterize the structures of biomolecules, large and small. He joined the chemistry faculty at the University of Washington in 2011, where he also participates in several interdisciplinary programs. His research group develops MS-based approaches for elucidating the structures, stabilities, and dynamics of biomolecules. They apply those approaches to a wide range of biological systems, especially those involved in protein homeostasis.

Hosted by Professor Varun Gadkari