Professor Helen Cooper is an expert in the gas-phase ion chemistry of peptides and proteins. She is a world-leader in the field of electron capture dissociation mass spectrometry and is responsible for establishing the University of Birmingham as a centre of excellence in mass spectrometry research. She will talk to us about her award-winning recent work in a lecture entitled: "Native ambient mass spectrometry: In situ analysis of proteins in tissue" (an abstract is given further down the page).
Doors will open at 6.00 pm for refreshments before the lecture begins at 6.30 pm.
The event will be held in the Department of Chemistry at the University of York. Information about travel to the University of York and parking on campus is available here: https://www.york.ac.uk/about/transport-maps-parking/parking/
Registration for the event will open on 1st February 2024, and tickets can be booked here: https://www.eventbrite.co.uk/e/joint-rsc-rsb-symposium-2024-tickets-707670450367?aff=oddtdtcreator
Abstract for talk:
Native ambient mass spectrometry (NAMS) combines native mass spectrometry, an established technique in structural biology, and ambient mass spectrometry, in which biological substrates such as thin tissue sections are analysed directly with little or no sample preparation. The combined benefits of NAMS for analysis of protein assemblies and protein-ligand complexes include measurement of accurate mass and stoichiometry, identification of both protein and non-covalently bound ligands, together with information on spatial distribution. Recent efforts using liquid extraction surface analysis (LESA) and nanospray desorption electrospray ionization (nano-DESI), have advanced NAMS for the analysis of fresh frozen issue, allowing the spatial distribution of protein assemblies to be mapped. Endogenous protein assemblies and their constituents (including small molecule ligands) can be identified by top-down dissection of assemblies in the gas phase, potentially allowing the discovery of new protein-ligand interactions.
In this presentation, recent developments in NAMS will be discussed, including the analysis of integral membrane proteins and membrane-associated proteins, characterisation of protein-drug complexes formed in vivo, and application of NAMS for understanding the molecular mechanisms involved in the fatal neurodegenerative disease amyotrophic lateral sclerosis.
Doors will open at 6.00 pm for refreshments before the lecture begins at 6.30 pm.
The event will be held in the Department of Chemistry at the University of York. Information about travel to the University of York and parking on campus is available here: https://www.york.ac.uk/about/transport-maps-parking/parking/
Registration for the event will open on 1st February 2024, and tickets can be booked here: https://www.eventbrite.co.uk/e/joint-rsc-rsb-symposium-2024-tickets-707670450367?aff=oddtdtcreator
Abstract for talk:
Native ambient mass spectrometry (NAMS) combines native mass spectrometry, an established technique in structural biology, and ambient mass spectrometry, in which biological substrates such as thin tissue sections are analysed directly with little or no sample preparation. The combined benefits of NAMS for analysis of protein assemblies and protein-ligand complexes include measurement of accurate mass and stoichiometry, identification of both protein and non-covalently bound ligands, together with information on spatial distribution. Recent efforts using liquid extraction surface analysis (LESA) and nanospray desorption electrospray ionization (nano-DESI), have advanced NAMS for the analysis of fresh frozen issue, allowing the spatial distribution of protein assemblies to be mapped. Endogenous protein assemblies and their constituents (including small molecule ligands) can be identified by top-down dissection of assemblies in the gas phase, potentially allowing the discovery of new protein-ligand interactions.
In this presentation, recent developments in NAMS will be discussed, including the analysis of integral membrane proteins and membrane-associated proteins, characterisation of protein-drug complexes formed in vivo, and application of NAMS for understanding the molecular mechanisms involved in the fatal neurodegenerative disease amyotrophic lateral sclerosis.
