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Applied Mass Spectrometry @ McGill - Macdonald Campus:

THIS SEMINAR HAS BEEN POSTPONED

Special seminar by Dr. Christopher Thibodeaux, Department of Chemistry, 香蕉视频.

This lecture will focus on the application of mass spectrometry to study the involvement of protein conformational changes in biosynthetic enzyme function. Specifically, I will discuss the use of hydrogen/deuterium exchange mass spectrometry (HDX-MS) and native mass spectrometry coupled to ion mobility separations. HDX-MS measures how perturbations (substrate binding, mutagenesis, etc.) alter the exchange rate of solvent deuterium into the backbone amide moiety of proteins. This exchange rate is largely a function of protein secondary structure and, thus, provides information on the location of substrate binding sites and other perturbation-induced structural changes in the protein. In native mass spectrometry, proteins (or non-covalently bound protein-substrate complexes) are transferred from solution into the gas phase in a natively folded state using nano-electrospray ionization. Once in the gas phase, the conformational distribution of the folded protein can be probed by ion mobility separations. The parameters derived from these measurements can then be correlated to structural parameters derived from other techniques in order to build mechanistic models for the involvement of protein conformational changes in enzyme function. Finally, I will discuss how my lab is applying HDX-MS and native MS approaches to study the multifunctional enzymes involved in peptide natural product biosynthesis.

Everyone is welcome to attend.