Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published March 2013 | Accepted Version + Submitted
Journal Article Open

Directional interactions and cooperativity between mechanosensitive membrane proteins

Abstract

While modern structural biology has provided us with a rich and diverse picture of membrane proteins, the biological function of membrane proteins is often influenced by the mechanical properties of the surrounding lipid bilayer. Here we explore the relation between the shape of membrane proteins and the cooperative function of membrane proteins induced by membrane-mediated elastic interactions. For the experimental model system of mechanosensitive ion channels we find that the sign and strength of elastic interactions depend on the protein shape, yielding distinct cooperative gating curves for distinct protein orientations. Our approach predicts how directional elastic interactions affect the molecular structure, organization, and biological function of proteins in crowded membranes.

Additional Information

© 2013 EPLA. Received 18 January 2013; accepted 25 February 2013; published online 26 March 2013. This work was supported at USC by the National Science Foundation through NSF award number DMR-1206332 and at Caltech by a Collaborative Innovation Award of the Howard Hughes Medical Institute, and the National Institutes of Health through NIH award number R01 GM084211 and the Director's Pioneer Award. We thank C. L. Henley, W. S. Klug, M. Lindén, D. C. Rees, and N. S. Wingreen for helpful comments.

Attached Files

Accepted Version - nihms494041.pdf

Submitted - 1209.3083v2.pdf

Files

nihms494041.pdf
Files (3.0 MB)
Name Size Download all
md5:76e82f79a9d1c9d225606a5cb3190dce
1.8 MB Preview Download
md5:62a6aa3d82486445734912035d47ca79
1.2 MB Preview Download

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023