|Download: This Video|
|Resources: Related Articles|
|Trouble Viewing? Try it on iTunes.Report a problem.|
Mass spectrometry is a powerful tool for elucidating the elemental composition of a sample or molecule. More recently, it has been used to characterize biological material, in particular proteins and protein complexes, in a variety of organisms. In this lecture, we will review the underlying principles of how a mass spectrometer works, discuss up to date instrumentation that is presently being used in the biological research setting and provide specific examples of how mass spectrometry is being used to reveal functional insight into different biological systems.
Nevan Krogan is a professor in the Department of Cellular and Molecular Pharmacology at the University of California-San Francisco (UCSF). He obtained his PhD from the University of Toronto in 2006 and became a Sandler Fellow at UCSF prior to becoming an assistant professor.
His research, which is in the area of functional genomics/proteomics and systems biology, is focused on the generation and analysis of large-scale genetic and protein-protein interaction datasets in a variety of organisms, ranging from bacteria to mammalian cells. To this end, he has developed strategies that were used to generate quantative genetic interaction maps and has been involved in affinity tag/purification/mass spectrometry approaches to create protein-protein interaction maps.
He uses these unbiased, global datasets to extract the details of how individual pathways, complexes and proteins function, most notably in nuclear processes such as transcription, DNA repair/replication and chromatin regulation.
- Stephen Mayo iBioSeminar: Computational Protein Design
The abc's (and xyz's) of peptide sequencing, Nature Reviews Molecular Cell Biology, 5, 699-711, 2004.
Analysis of protein complexes using mass spectrometry, Nature Reviews Molecular Cell Biology, 8, 645-654, 2007.
Applying mass spectrometry-based proteomics to genetics, Nature Reviews Genetics, 10, 617-627, 2009.