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VERSION:2.0
PRODID:-//RLASKEY//CALENDEROUS//EN
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VEVENT
DTSTAMP:20260912T123444Z
LAST-MODIFIED:20191021T162620Z
DTSTART:20191029T180000Z
DTEND:20191029T190000Z
UID:event2218@bu.edu
URL:http://physics.bu.edu/internal/events/show/2218
SUMMARY:Bioengineering and Analysis of Near-Infrared Absorbing Optogenetic 
	Rhodopsins
DESCRIPTION:Featuring Gaoxiang Mei\n\nPart of the Preliminary Oral Exam.\n\
	nExamining Committee: Kenneth Rothschild\, Shyam Erramilli\, Claudio Chamon
	\, Robert Carey  \n\n\n\nAbstract:\n\nOptogenetics is a biological techniqu
	e that allows researchers to control neuronal activity with light. It has b
	een applied in a variety of important fields such as probing the role of in
	dividual neurons in the brain. Neuronal control in optogenetics is achieved
	 using optogenetic actuators like microbial rhodopsins.  However\, effectiv
	e in vivo optogenetics is in many cases severely limited due to the strong 
	absorption and scattering of visible light by biological tissues. Recently\
	, a combination of opsin site-directed mutagenesis and analog retinal subst
	itution has produced variants of microbial rhodopsins which absorb maximall
	y in the near-infrared (NIR). One class of such microbial rhodopsins discov
	ered in marine proteobacteria\, called proteorhodopsins (PRs)\, have divers
	e functions including serving as light-driven proton pumps. Although PRs ha
	ve been engineered for use in a variety of biotechnological applications\, 
	the molecular mechanism underlying their function is not fully understood. 
	 Better understanding of their mechanism would facilitate bioengineering of
	 PRs’ properties such as the wavelength of absorption for specific applic
	ations. This talk will first cover resonance Raman and FTIR-difference spec
	troscopy that helped elucidate the molecular mechanism of bacteriorhodopsin
	\, the first microbial rhodopsin to be studied.   Then latest results from 
	UV-Visible-NIR absorption and resonance Raman spectroscopy will be presente
	d on green absorbing proteorhodopsin (GPR) and its mutants\, which exhibit 
	some similarities with bacteriorhodopsin.  Utilizing the red-shifted double
	 mutant D212N/F234S and the substitution of native A1 retinal with analog r
	etinal 3-methylamino-16-nor-1\,2\,3\,4-didehydroretinal (MMAR)\, a dramatic
	 red-shift of approximately 200 nm is achieved with this GPR-DNFS:MR. The t
	alk will end with an outline of future work on other optogenetic proteins s
	uch as the florescent voltage sensing archaerhodopsin-3 (AR3) and its mutan
	ts.
LOCATION:SCI 352\, 590 Commonwealth Avenue\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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