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DTSTART:19960101T000000 END:STANDARD BEGIN:STANDARD TZNAME:GMT TZOFFSETFROM:+0100 TZOFFSETTO:+0000 DTSTART:19961027T020000 RRULE:FREQ=YEARLY;BYMONTH=10;BYDAY=-1SU END:STANDARD END:VTIMEZONE BEGIN:VEVENT DTSTAMP:20260614T012920Z DTSTART;VALUE=DATE-TIME:20170927T130000 DTEND;VALUE=DATE-TIME:20170927T140000 SUMMARY:Seminar by Professor Mohan Balasubramanian and Professor Robert C ross\, Division of Biomedical Sciences\, ÌÇÐÄTV Medical School TZID:Europe/London UID:20170927-8a17841a5e514a5d015e5b999bb24dab@warwick.ac.uk CREATED:20170907T090907Z DESCRIPTION:'Cytokinesis in vitro and in vivo' by Professor Mohan Balasub ramanian\, Pro Dean (Research) What I cannot create\, I do not understan d – Richard Feynman We are interested in understanding mechanisms drivin g division of eukaryotic cells from one to two. This process requires an actin and myosin II containing ring\, whose contraction generates tensi on required for cell division. Over the past three decades\, we have ide ntified and characterised gene products involved in cytokinetic ring ass embly and together with work of other colleagues in the field we have a reasonably good understanding of ring assembly mechanisms. We are now fo cusing on the mechanisms of actomyosin ring contraction a in vitro appro ach\, which has required combining approaches of biophysics\, biochemist ry\, chemistry\, genetic code expansion\, and more. We are also working towards reconstituting actomyosin ring assembly using purified component s and model membranes. We believe this work will both illuminate mechani sms of cell division and expound the design principles behind assembly a nd function of force generating cell division machines. 'Allostery in mi crotubules' by Professor Robert Cross\, Professor of Mechanochemical Cel l Biology Allostery\, in which the binding of an effector switches a pro tein from one global conformation to another\, was discovered and much-s tudied in the classical era of molecular biology. Influential models tha t accounted quantitatively for the switching behaviour were constructed. More recently\, it has been realised that allostery can happen even in natively unfolded proteins. This has lead to a new and wider view of all ostery in which effectors serve to bias conformational dynamics\, rather than flipping a conformational switch. It has also been realised that a llosteric transitions occur in large ensembles of linked protein subunit s. We and others are interested in allostery in microtubules\, polymers of typically thousands of subunits in which dynamics and conformation an d even geometry can all vary according to which effectors bind\, and con versely\, effector proteins can sense and respond to the local structure and conformation of the microtubule lattice. To really understand how m icrotubules work in complex in vivo contexts\, we need to understand the range and power of these allosteric effects. Recent work in the group h as used cryoEM (collab. with Carolyn Moores lab) to look at near-atomic resolution at the conformation of S. pombe MTs in complex with Mal3\, in relation to the effects of Mal3 on dynamic instability. Dan Peet has bu ilt a microfluidics framework for Nick Carter’s WOSM\, and used it to lo ok by TIRF-STORM at the effects of kinesin on the lattice spacing and dy namics of MTs. Algirdas Toleikis is looking at the effect of different M T lattices on the propensity of kinesin-1 to take backsteps. Naomi Shepp ard is expressing and purifying mutant tubulins\, aiming ultimately to u nderstand the sequence determinants for allosteric drugs. LOCATION:GLT3\, ÌÇÐÄTV Medical School CATEGORIES:BiomedicalSciences,DivisionalSeminars LAST-MODIFIED:20170927T073635Z ORGANIZER;CN=Jas Bains: END:VEVENT END:VCALENDAR