BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Talks.cam//talks.cam.ac.uk//
X-WR-CALNAME:Talks.cam
BEGIN:VEVENT
SUMMARY:The diverse and expanding role of mass spectrometry in structural 
 and molecular biology - Albert Heck\, Professor of Biomolecular Mass Spect
 rometry and Proteomics\, Utrecht University
DTSTART:20200420T100000Z
DTEND:20200420T110000Z
UID:TALK140728@talks.cam.ac.uk
CONTACT:Scientific Meetings Co-ordinator
DESCRIPTION:Mass Spectrometry based proteomics plays a pivotal role in rev
 ealing the plethora of protein interactions that take place inside a cell\
 , wherein proteins form protein assemblies and/or signalling networks. Esp
 ecially using affinity purification of tagged proteins followed by mass sp
 ectrometric analysis of its binding partners a wealth of data has been gat
 hered. \nA next step will be to gather more in-depth structural and functi
 onal information on all these individual assemblies. This may come from in
 -depth high-resolution structural models\, as well as detailed information
  on how they function and dynamically evolve during cellular perturbations
 . \nMass spectrometry can also contribute to this next level of protein in
 teraction analysis although it does require partly different and novel app
 roaches. To contribute to this emerging new area in structural proteomics\
 , our group is developing new methods using native mass spectrometry and c
 ross-linking mass spectrometry with the aim to bridge the gap between inte
 raction proteomics and structural biology. These new innovations and appli
 cations of them in interaction proteomics will be central in my presentati
 on.\n\nIn the first part of the talk native mass spectrometry and its appl
 ications in probing\nlarge and dynamic protein assemblies and protein inte
 ractions will be described\, focusing on the analysis of ribosomal particl
 es\, viruses and complexes involved in our immune response. We aim to expa
 nd the boundaries of mass spectrometry in mass range up to several million
  Da\, sensitivity and mass resolution\, and are now able to detect and ana
 lyse single particles/molecules.\n\nIn the second part I will highlight re
 cent work on cross-linking mass spectrometry. We have developed XL-MS meth
 ods aimed at probing protein interactions at the proteome wide level. We d
 emonstrate the power of our novel strategy to organelles such as mitochond
 ria and nuclei. In each of these studies we successfully identified thousa
 nds of cross-links. Many of the identified cross-links could be validated 
 by mapping them on available high-resolution structures\, but the data als
 o provide information on assemblies for which no high-resolution structure
 s are available\, and even reveal new protein interaction networks.\n\nIn 
 the final part of my talk I will briefly describe a new view at the plasma
  proteome\, whereby I will address the questions\; Are our plasma proteome
 s all unique? and ultimately What is a protein? \n
LOCATION:Max Perutz Lecture Theatre\, MRC Laboratory of Molecular Biology
END:VEVENT
END:VCALENDAR