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PRODID:-//UIC
BEGIN:VEVENT
UID:2026041810482620091203T11000020091203T12000069e40a3a9c94e@uic.edu
CATEGORIES:MEETING
STATUS:TENTATIVE
DTSTAMP:20190617T074929
DTSTART;VALUE=DATE:20091203
SUMMARY:Ursula Perez-Salas, UIC
DESCRIPTION:Towards Understanding Self Assembled Morphologies of Amphiphilic Mixtures in Aqueous Environments for Membrane Protein Crystallization Applications: the Bicelle-based Method  Abstract:  Crystallizing of membrane proteins for structure determination is a challenge. In contrast to soluble proteins, their hydrophobic moieties have been demonstrated to add a significant level of complexity which has resulted in a number of known structures significantly smaller than those of soluble proteins: 200 vs 60000. A relatively new method to crystallize membrane proteins is the bicelle-based method. Well-diffracting crystals of bacteriorhodopsin and some G-protein coupled receptors have been obtained by this method. The bicelle-based method can potentially prove to be robust enough to allow for more membrane proteins to be crystallized, because bicelles offer a significant variety of membrane-like environments. The key to making it a reliable methodology is to understand how the lipid-detergent scaffold promotes the nucleation and growth of protein crystals. | Event post: https://che.uic.edu/events?page_id=1298
LOCATION:CEB 230 810 South Clinton Street  Chicago IL 60612
CLASS:PRIVATE
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