Bulletin of the American Physical Society
APS March Meeting 2012
Volume 57, Number 1
Monday–Friday, February 27–March 2 2012; Boston, Massachusetts
Session A41: Focus Session: Structure and Dynamics of Membranes
8:00 AM–11:00 AM,
Monday, February 27, 2012
Sponsoring Units: DBIO DPOLY DMP
Chair: Mu-Ping Nieh, University of Connecticut
Abstract ID: BAPS.2012.MAR.A41.1
Abstract: A41.00001 : A Neutron View of Proteins in Lipid Bilayers*
8:00 AM–8:36 AM
Preview Abstract Abstract
(University of California at Irvine, Dept. of Physiology and Biophysics)
Despite the growing number of atomic-resolution membrane protein structures, direct structural information about proteins in their native membrane environment is scarce. This problem is particularly relevant in the case of the highly-charged S1-S4 voltage- sensing domains responsible for nerve impulses, where interactions with the lipid bilayer are critical for the function of voltage-activated potassium channels. We have used neutron diffraction, solid-state nuclear magnetic resonance spectroscopy, and molecular dynamics simulations to investigate the structure and hydration of bilayer membranes containing S1-S4 voltage-sensing domains. Our results show that voltage sensors adopt transmembrane orientations, cause a modest reshaping of the surrounding lipid bilayer, and that water molecules intimately interact with the protein within the membrane. These structural findings reveal that voltage sensors have evolved to interact with the lipid membrane while keeping the energetic and structural perturbations to a minimum, and that water penetrates into the membrane to hydrate charged residues and shape the transmembrane electric field.
*Research supported in part by PO1 GM86685 from NIGMS and NINDS.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2012.MAR.A41.1
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