Ion mobility mass spectrometry - measuring more than mass
Dates: | 6 March 2014 |
Times: | 09:00 - 10:00 |
What is it: | Seminar |
Organiser: | Faculty of Life Sciences |
Who is it for: | University staff |
Speaker: | Perdita Barran |
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A Gene Regulation and Biotechnology Seminar
The analytical advantages of mass spectrometry apply to its use to examine intact proteins and complexes and there is an emerging research field that identifies proteins this way – so called “top-down” methodologies where proteins are sequenced in their entirety in the mass spectrometer. Most top down approaches destroy the functional form of the protein prior to sequencing, to enable higher throughput and to facilitate more productive analysis from higher charged parent ions. This is not the route we take, rather we aim to probe intact proteins and complexes , with careful use of nano-electrospray ionisation (nESI) to retain solution structures. Native mass spectrometry provides information about tertiary and quaternary structure, and intramolecular interactions. This talk will discuss recent results from our lab with an emphasis on understanding protein structure and dynamics.
Speaker
Perdita Barran
Organisation: Michael Barber centre for collaborative mass spectrometry, Dept of Chemistry
Travel and Contact Information
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1.006
AV Hill Building
Manchester