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VERSION:2.0
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METHOD:PUBLISH
BEGIN:VEVENT
DTSTAMP:20260817T214452Z
LAST-MODIFIED:20121116T203436Z
DTSTART:20090226T200000Z
DTEND:20090226T210000Z
UID:event404@bu.edu
URL:http://physics.bu.edu/internal/events/show/404
SUMMARY:Mechanical Design of the Kinesin Motor
DESCRIPTION:Featuring Wonmuck Hwang\, Texas A & M\nHosted by: Shyamsunder E
	rramilli\n\nPart of the Biophysics/Condensed Matter Seminar Series.\n\nAbst
	ract:\nA longstanding question about conventional kinesin\, the smallest bi
	pedal motor protein known to date\, is the mechanochemical amplifier: How i
	t converts the chemical energy associated with adenosine triphosphate (ATP)
	 into mechanical work. Using molecular dynamics simulations and structural 
	analyses\, we found that force is generated by a dynamic folding transition
	 of a mechanical element. Binding of an ATP molecule on the motor head atta
	ched to the microtubule track\, triggers folding of a beta-sheet domain nam
	ed the cover-neck bundle. The cover-neck bundle possesses a conformational 
	bias necessary to propel the other stepping head forward. Single-molecule m
	otility measurements on mutant kinesins designed to possess altered force-g
	enerating capacities support the cover-neck bundle mechanism. Identificatio
	n of the dynamic force-generating element makes it possible to control moti
	lity of kinesin\, which is a major intracellular cargo carrier as well as a
	 rising target for pharmaceutical and biotechnological applications.
LOCATION:SCI 352\, 590 Commonwealth Avenue\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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