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BEGIN:VEVENT
DTSTAMP:20260503T212117Z
DTSTART;VALUE=DATE-TIME:20250430T131500
DTEND;VALUE=DATE-TIME:20250430T141500
SUMMARY:BMS Seminar: Single-molecule studies of RNA virus replication\, D
 r Nicole Robb\; Interlocking nanomechanics of kinesin and microtubules\,
  Professor Robert Cross
TZID:Europe/London
UID:20250430-8ac672c593d938f50193da785c1f1b76@warwick.ac.uk
CREATED:20250314T092258Z
DESCRIPTION:Single-molecule studies of RNA virus replication Dr Nicole Ro
 bb\, Associate Professor\, Biomedical Sciences Directorate Abstract: RNA
  viruses are a major cause of morbidity and mortality in both humans and
  animals\, and result in a significant health and economic burden worldw
 ide. Our group uses a range of single-molecule microscopy techniques to 
 study RNA virus replication\, their morphology\, and to develop novel me
 thods for their diagnosis. In this talk I’ll describe our work using sin
 gle-molecule FRET\, a molecular ruler used to measure inter-protein and 
 RNA-RNA interactions\, to study influenza and SARS-CoV-2 replication com
 plexes\, and how these assays can be used to provide information on repl
 ication dynamics and the mechanism of antiviral inhibitors. ---- Interlo
 cking nanomechanics of kinesin and microtubules Professor Robert Cross\,
  Biomedical Sciences Directorate Abstract: Kinesins are microtubule-base
 d cargo transporters whose activities are central to the self-organisati
 on of eukaryotic cells and organisms. The archetype of the kinesin super
 family is kinesin-1. Kinesin-1 motors haul cargo towards the plus ends o
 f microtubules\, using a walking action in which the twin heads of each 
 molecule interact alternately with the microtubule. We are interested in
  this stepping mechanism\, and in that of other members of the kinesin f
 amily of molecular motors\, which is ancient and highly diverse. We have
  so far tended to concentrate mostly on the problem of how kinesins work
  as molecular machines\, attacking this problem using protein engineerin
 g and single molecule optical trapping. More recently\, we have realized
  that there is appreciable crosstalk between kinesin and tubulin\, the b
 uilding block for microtubules. Not only kinesin\, but also a number mic
 rotubule-associated proteins (MAPS) and a number of drugs\, including cr
 ucially-important cancer drugs like taxol\, can change the structure of 
 microtubules - and changes to the structure of microtubules can\, as we 
 now realize\, feed back to determine the speed\, power and directionalit
 y of kinesin stepping. I will present results from some of our newest ex
 periments\, designed to explore how structural switching of microtubules
  feeds back on kinesin stepping\, and vice versa.
LOCATION:IBRB Lecture Theatre
CATEGORIES:BiomedicalSciences,Directorate Seminars
LAST-MODIFIED:20250314T092258Z
ORGANIZER;CN=Jas Bains:
END:VEVENT
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