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BEGIN:VEVENT
DTSTAMP:20260918T221833Z
LAST-MODIFIED:20150220T164847Z
DTSTART:20150226T180000Z
DTEND:20150226T190000Z
UID:event1412@bu.edu
URL:http://physics.bu.edu/internal/events/show/1412
SUMMARY:Vibrational Spectroscopy of Optogenetic Rhodopsins
DESCRIPTION:Featuring Adrian Yi\n\nPart of the Preliminary Oral Exam.\n\nEx
	amining Committee: Kenneth Rothschild\, Shyamsunder Erramilli\, Tulika Bose
	\, Carter Cornwall\, Claudio Rebbi\n\nAbstract: Optogenetics is a new appro
	ach that allows researchers to control neuronal activity with light.  It is
	 currently being used by neuroscientists for a variety of decisive applicat
	ions such as probing the role of individual neurons in the brain.  It also 
	offers potential treatments for a variety of neurological disorders such as
	 Parkinson's disease.  A first step is the genetic targeting and expression
	 of light-sensitive proteins called microbial rhodopsin in the plasma membr
	ane of neurons of interest.  One class of such microbial rhodopsins found i
	n green algae\, called channelrhodopsin (ChRs)\, functions as light-activat
	ed cation channels.  In the resting state\, light absorption by ChRs allows
	 passive flow of cations into the neuron\, raising the membrane potential (
	depolarization) and thus triggering an action potential.  Although ChRs are
	 widely used in neuroscience\, the molecular mechanism underlying their fun
	ction is not fully understood.  Such basic knowledge would facilitate bioen
	gineering of ChRs’ properties such as the wavelength of absorption\, kine
	tics\, and cation selectivity for specific applications.  This talk will fi
	rst review the use of resonance Raman spectroscopy and FTIR-difference spec
	troscopy that helped elucidate the molecular mechanism of bacteriorhodopsin
	\, a light-driven proton pump\, at the level of individual amino acids and 
	internal water molecules.  The latest results will then be presented on cha
	nnelrhodopsin-1 from Chlamydomonas augustae (CaChR1)\, a cold-adapted alga 
	which exhibits some similarities with bacteriorhodopsin.  The talk will end
	 with an outline of future work on other optogenetic proteins such as the f
	lorescent voltage sensing archaerhodopsin-3 and its mutants.\n\n![Adrian](/
	resources/event-image/1412/0b10629_small)
LOCATION:PRB 365\, 3 Cummington Mall\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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