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BEGIN:VEVENT
DTSTAMP:20260912T174242Z
LAST-MODIFIED:20141203T202336Z
DTSTART:20141209T160000Z
DTEND:20141209T170000Z
UID:event1365@bu.edu
URL:http://physics.bu.edu/internal/events/show/1365
SUMMARY:Evolutionary Design Principles for Cellular Systems
DESCRIPTION:Featuring Dr. Kimberly Reynolds\, The University of Texas South
	western Medical Center\nHosted by: Plamen Ivanov\n\nPart of the Biophysics/
	Condensed Matter Seminar Series.\n\nAbstract:\nCellular function and fitnes
	s depends on the cooperative action of many proteins. Allosteric regulation
	\, the formation of physical complexes\, and the organization of enzymes in
	to metabolic cascades represent several ways in which proteins can be funct
	ionally coupled to one another to produce useful cellular behaviors.  How a
	re such functional interactions between proteins encoded at the amino acid 
	level\, and how do they evolve?  Statistical analysis of amino acid co-evol
	ution in individual protein domains reveals a general architecture for natu
	ral proteins in which sparse networks of amino acids underlie basic aspects
	 of structure and function.  These networks\, now termed sectors\, form phy
	sically contiguous pathways embedded in the tertiary structure. Using the m
	etabolic enzyme dihydrofolate reductase (DHFR) as a model system\, we show 
	that (1) sector-connected residues on the protein surface are hot spots for
	 the gain of allosteric regulation and (2) the sector of DHFR co-evolves wi
	th a second\, epistatically coupled metabolic protein. These findings sugge
	st practical guidelines for the engineering of new allosteric systems\, per
	mit description of a plausible model for the evolution of intermolecular co
	mmunication\, and motivate a global analysis of evolutionary couplings betw
	een proteins in cellular systems.
LOCATION:SCI 352\, 590 Commonwealth Avenue\, 02215
STATUS:CONFIRMED
CLASS:PUBLIC
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