Dec 3 2009

Ursula Perez-Salas, UIC

December 3, 2009


CEB 230


810 South Clinton Street, Chicago, IL 60612

Towards Understanding Self Assembled Morphologies of Amphiphilic Mixtures in Aqueous Environments for Membrane Protein Crystallization Applications: the Bicelle-based Method

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.


UIC Chemical Engineering

Date posted

Jun 17, 2019

Date updated

Jun 17, 2019