Office Location: Cyclotron/Mass Spectrometry 101
Mailing Address: Campus Box 1134
Office Phone: (314) 935-4814
Lab Phone: (314) 935-7485
Fax: (314) 935-7484
Email Address: email@example.com
Michael L. Gross is a chemist who has worked independently in mass spectrometry since 1968. He began his career at the University of Nebraska-Lincoln, where he was distinguished professor of chemistry and director of an NSF Center for Mass Spectrometry until 1994. He moved to Washington University in 1994 as professor of chemistry and principal investigator of the WU NIH NIGMS Mass Spectrometry Research Resource. Dr. Gross is a highly cited chemist who has won the American Chemical Society Field and Franklin Award and the Midwest Award. He awarded the JJ Thomson Medal and the Eastern Analytical Symposium Award for Distinguished Contributions to Mass Spectrometry and the Commonwealth of Massachusetts Pioneer Award for “In Search of the Health Consequences of Dioxin in Our Environment.” He was honored by the Washington University Graduate Student Senate with the Outstanding Mentor Award in 2001. He is founding editor of the Journal of the American Society for Mass Spectrometry, coeditor of the “Encyclopedia of Mass Spectrometry” (published by Elsevier), and was editor until 1990 of Mass Spectrometry Reviews. He has served on numerous editorial boards and as a consultant to industry and academic laboratories.
Gross’ research focuses mainly on the development of mass spectrometry (MS) in biophysics, specifically to probe protein-ligand interaction interfaces, affinities, and folding/unfolding. The work includes both instrument and method development and application to important proteins and protein complexes. In biophysics, his group is interested in protein footprinting whereby they investigate protein hydrogen-deuterium exchange (HDX) coupled with fast digestion. Here they contributed a method for determination of protein/ligand interactions by titration and HD exchange (PLIMSTEX). Another approach to footprinting that his group developed is fast photochemical oxidation of proteins (FPOP) using a pulsed laser. The approach maps protein binding regions at the peptide and sometimes amino-acid levels on the microsecond timescale by using reactions with hydroxide and other radicals. The speed of this latter approach permits them to follow fast protein folding/unfolding in a T-jump experiment. His research group also employs specific chemical reagents to footprint proteins and determines their interfaces and orientations in complex biological settings.
They also are interested in top-down MS-based protein sequencing via electron capture and FTICR MS and ion mobility and are using it to investigate protein assemblies and therapeutic proteins. They showed this approach can give long runs of protein sequence from flexible regions of the protein, thus allowing identification of constituent proteins, their interfaces, and their less structured regions. They have contributed extensively to Fourier transform ICR mass spectrometry, especially electrical compensation of ICR traps, accurate mass measurements, laser desorption, and ion chemistry, and they continue the work with trap compensation and ion activation.
The ability of the Gross group to develop and utilize new MS technology and methods attracts many collaborators, with whom they study systems relevant to photosynthesis and to immunology, diabetes, cancer, AIDS, Alzheimer’s and other diseases, sometimes collaborating to make proteomics measurements.