Membrane proteins are difficult to structurally characterize due to its instability when they are solubilized in detergent.  In order to overcome this problem, we are developing a new method to structurally characterize membrane proteins in a lipid bilayer.  By inserting membrane proteins in a highly curved and compact lipid bilayer, we have made membrane proteins to arrange in a polyhedral configuration which we named as a membrane protein polyhedron (MPP).  We have successfully created MPPs of E. coli mechanosensitive channel of small conductance (MscS) in a 1,2-dimyristoyl- n-glycero-3-phosphocholine bilayer. Using electron microscopy, we have characterized that MscS MPPs form 50 nm diameter particles.  Furthermore, using EM tomography, we were able generate the envelope of MscS MPPs and dock 18 MscS molecules.  We determined that 18 MscS are arranged in a snub cuboctahedron configuration.

Structural characterization of <i>Escherichia coli</i> MscS membrane protein polyhedra

241st National Meeting (2011)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Structural characterization of Escherichia coli MscS membrane protein polyhedra