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BEGIN:VEVENT
DTSTAMP:20261004T132752Z
LAST-MODIFIED:20121116T203436Z
DTSTART:20110208T203000Z
DTEND:20110208T213000Z
UID:event699@bu.edu
URL:http://physics.bu.edu/internal/events/show/699
SUMMARY:Some Surprises in the Biophysics of Protein Dynamics
DESCRIPTION:Featuring Vijay Pande\, Stanford University\nHosted by: Shyamsu
	nder Erramilli\nPoster: http://physics.bu.edu/posters/2011_Spring/02_Pande.
	pdf\n\nPart of the Physics Department Colloquia Series.\n\nAbstract:  The s
	elf-assembly of proteins ("protein folding") is one of the key steps in the
	 function of proteins\, such as enzymes and antibodies.  The mechanism by w
	hich this assembly occurs has been an outstanding question in molecular bio
	physics and biophysical chemistry for decades.  Also\, protein misfolding h
	as been linked to numerous diseases\, such as Alzhemier's and Huntington's 
	Disease.  Over the last 5 years\, there has been tremendous progress in our
	 ability to understand protein dynamics\, such as folding in atomic detail.
	  With the latest technology utilizing worldwide distributed computing ("Fo
	lding@home")\, we can directly simulate the folding of proteins on the 80 r
	esidue scale on the 10’s of millisecond timescale in all-atom detail.  On
	e can also use these methods to study folding in the presence of biological
	 machinery\, such as inside chaperonins or the ribosome tunnel.  Moreover\,
	 a new mechanistic framework has provided a new framework for simulating an
	d conceptualizing protein folding\, leading to a new analytic statistical m
	echanics theory for protein folding kinetics.  The picture that is emerging
	 suggests a change in how we conceptualize protein dynamics in general\, in
	cluding protein folding and misfolding\, including new roles for non-native
	 interactions\, novel mechanisms for folding and misfolding\, and new thoug
	hts for the role of water in protein folding in vivo.
LOCATION:SCI 107\, 590 Commonwealth Avenue\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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