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SUMMARY:Collisions of Large Non-Covalent Complexes into Surfaces : An MS-B
 ased Structural Biology Tool
DTSTART:20160922T163000
DTEND:20160922T173000
DTSTAMP:20260511T073004Z
UID:2437007b8fd72358e9c5f2694c3a2fcd8229b8033251c6ef0fee6318
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Vicki Wysocki\nOhio State University\nDepartment of Chem
 istry and Biochemistry\nCharacterization of the overall topology and inter
 -subunit contacts of protein complexes\, and their assembly/disassembly an
 d unfolding pathways\, is critical because protein complexes regulate key 
 biological processes\, including processes important in understanding and 
 controlling disease.  Conventional structural biology methods such as X-r
 ay crystallography\, nuclear magnetic resonance\, and cryo-electron micros
 copy provide high-resolution information on the structures of protein comp
 lexes and are the gold standards in the field. However\, other emerging bi
 ophysical methods that provide lower resolution data (e.g. stoichiometry a
 nd subunit connectivity) on the structures of the protein complexes are al
 so important.  Native mass spectrometry is an approach that provides crit
 ical structural information with high throughput on low sample amounts.  
 The power of native MS increases when coupled to collisions of the large n
 on-covalent complexes with a target surface to cause dissociation of the c
 omplex into subcomplexes. Additional increases in information are seen by 
 coupling the surface collision experiment with ion mobility (IM-MS)\, a te
 chnique that measures rotationally averaged collisional cross sections and
  thus direct information on conformational changes\, or  high resolution 
 mass spectrometry (HRMS). This presentation illustrates surface-induced di
 ssociation/ion mobility (SID/IM) MS and SID/HRMS for characterization of t
 opology\, intersubunit connectivity\, and other structural features of mul
 timeric protein complexes.
LOCATION:CH G1 495 https://plan.epfl.ch/?room==CH%20G1%20495
STATUS:CONFIRMED
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