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Biochemistry Seminar: Michael L. Gross, "Role of Mass Spectrometry in Structural Proteomics and Biophysics"

Micheal L. Gross, Prof of Chemistry, Immunology, and Medicine, Dept of Chemistry, Washington University in ST. Louis, MO, "Role of Mass Spectrometry in Structural Proteomics and Biophysics"
When Mar 14, 2018
from 12:00 PM to 01:00 PM
Where CUNY ASRC Main Auditorium
Contact Name
Contact Phone 212-650-8803
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ABSTRACT

There is a compelling need for methods to characterize protein higher order structure and interactions especially when high resolution methods of X-ray crystallography, cryoEM, and NMR are not applicable, too slow or insensitive, or fail.  This need carries over in the development of protein therapeutics to meet the challenge that they, unlike small-molecule drugs, can exist in various higher order structures (HOS) and can oligomerize, compromising their efficacy as drugs.  Mass-spectrometry-based methods have high sensitivity, high information content, and fast turnaround, motivating their use for protein biophysics and therapeutic protein studies. We will show examples of native MS and electron-capture dissociation, HD amide exchange, specific amino-acid labeling, and fast photochemical oxidation of proteins (FPOP) that meet the challenge to assess the higher order structure and interactions of proteins.  These examples include (1) antibody-antigen interactions and epitope mapping, (2) protein folding as a function of pH and at high speed, (3) protein-small molecule binding and affinity, (4) mechanistic steps for oligomerization of amyloid proteins, and (5) footprinting membrane proteins in lipid Nanodics and in living cells among others.

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