Ursula Perez-Salas, UIC
December 3, 2009
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.
Date posted
Jun 17, 2019
Date updated
Jun 17, 2019