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UID:20250821T144300EDT-1028es2IA1@132.216.98.100
DTSTAMP:20250821T184300Z
DESCRIPTION:In this two-part talk\, I will discuss: 1) how enzymes dissipat
 e catalytic energy and 2) a solution to the 'single molecule counting prob
 lem'.1) Enzymes releasing heat: Enzymes are proteins that are responsible 
 for catalyzing reactions in living systems. Some enzymes perform reactions
  so exothermic that their ownself-generated heat would be sufficient to un
 fold over a million small proteins per second. How do enzymes then cope wi
 th this heat? Here I will discuss recent work with collaborators where we 
 have shown that enzymes rapidly dissipate heat by accelerating their cente
 r of mass.2) Counting problem: Characterizing protein assemblies — as they
  occur in their native cellular environment — is a major challenge since t
 hese assemblies can involve up to many tens of proteins within approximate
 ly a 10nm range. The method I present shows promise in characterizing prot
 ein complexes in living cells by using state-of-the-art (superresolution) 
 data already available. That is\, I will propose a solution to the countin
 g problem which involves determining how many proteins of type X\, say\, a
 re in a given complex in living cells. Addressing this problem is a first 
 step in quantitatively characterizing protein-protein interactions which i
 s an essential prerequisite for developing a mechanistic understanding of 
 cell biology and the disease states associated with defective protein comp
 lexes.
DTSTART:20160225T180000Z
DTEND:20160225T193000Z
LOCATION:Rm 10\, Maass Chemistry Building\, CA\, QC\, Montreal\, H3A 0B8\, 
 801 rue Sherbrooke Ouest
SUMMARY:Chemistry Department Seminar: Dr. Steve Presse\, Enzymes stepping o
 n landmines
URL:/chemistry/channels/event/chemistry-department-sem
 inar-dr-steve-presse-enzymes-stepping-landmines-257584
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