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UID:20250928T014323EDT-270163DPPu@132.216.98.100
DTSTAMP:20250928T054323Z
DESCRIPTION:Abstract:\n\nWithin each living organism proteins are at work\,
  carrying out activities which impact every aspect of cellular function fr
 om synthesis to cell death. The next generation of medicines will rely hea
 vily upon our ability to quickly assess the structures and stabilities of 
 such complex macromolecular machines\, as well as the influence of large l
 ibraries of conformationally-selective small molecule binders and protein-
 based biotherapeutics. Such endeavours are nearly insurmountable with curr
 ent tools. In this presentation\, I will discuss recent developments surro
 unding the activation of gas-phase protein complex ions aimed at bridging 
 this gap in basic technology. One such development is collision induced un
 folding (CIU)\, which uses ion mobility-mass spectrometry (IM-MS) to measu
 re the stability and unfolding pathways of gas-phase proteins\, without th
 e need for covalent labels or tagging\, and consuming 10-100 times less sa
 mple than almost any other label-free technology. In parallel with this ap
 proach\, my lab are pursuing chemical modification strategies aimed at the
  improved liberation of sequence informative peptide fragments from intact
  protein complex precursor ions during collision induced dissociation (CID
 )\, enabling the assessment of protein quaternary structure and sequence s
 imultaneously. Recent developments in understanding the mechanisms of prot
 ein CIU and CID\, the ability of these tools to differentiate therapeutic 
 antibodies and enable the discovery of conformationally-selective inhibito
 rs\, will be discussed.\n\nBio:\n\nBrandon T. Ruotolo currently holds the 
 rank of Professor with Tenure in the Department of Chemistry\, University 
 of Michigan. He earned his B.S. in Chemistry from Saint Louis University i
 n 1999. Brandon then received his Ph.D. from Texas A&M University in 2004 
 under the direction of David H. Russell. He did his post-doctoral work at 
 the University of Cambridge with Dame Carol V. Robinson\, and was awarded 
 the first ever Waters Research Fellowship in 2008. Brandon moved to the Un
 iversity of Michigan in 2009\, where he began his independent career.\n\nT
 he Ruotolo research group at the University of Michigan seeks to enable br
 eakthroughs in structural biology and drug discovery by leveraging the pot
 ential of ion mobility-mass spectrometry (IM-MS) for the comprehensive\, 3
 D structural analysis of the proteome. To this end\, Ruotolo and his team 
 have studied the role of solvation on biomolecular structure\, introduced 
 collision induced unfolding (CIU) - a new fingerprinting technology capabl
 e of detecting the structural state of protein-ligand complexes and biothe
 rapeutics\, developed software packages for the enhanced interpretation an
 d throughput of IM-MS and CIU data\, and investigated the structural conse
 quences of small molecule drug-like compounds upon binding amyloid peptide
 s. Ruotolo’s work has resulted in over 115 peer-reviewed publications\, an
 d many awards\, including the American Society for Mass Spectrometry Resea
 rch Award\, a National Science Foundation CAREER award\, the Eli Lilly You
 ng Investigator Award in Analytical Chemistry\, the Protein Society Young 
 Investigator Award\, and the Agilent Thought Leader Award.\n
DTSTART:20191105T180000Z
DTEND:20191105T193000Z
LOCATION:Room 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\
 , 801 rue Sherbrooke Ouest
SUMMARY:Chemical Society Seminar: Brandon Ruotolo - Gas-Phase Structural Bi
 ology: New Technologies for the Rapid Assessment of Protein Complex Sequen
 ce\, Structure\, and Stability
URL:/chemistry/channels/event/chemical-society-seminar
 -brandon-ruotolo-gas-phase-structural-biology-new-technologies-rapid-29960
 2
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