Hydration Dynamics as an Intrinsic Ruler for Refining Protein Structure at Lipid Membrane Interfaces

April 24, 2013

The structural properties of a membrane-associating protein at the water–membrane interfaces are intimately linked to its biological function, but they are difficult to characterize using existing biophysical tools. We identify the existence of a distinct intrinsic gradient of water diffusion across the lipid bilayer, encompassing a thick surface hydration layer above the lipid membrane surface, and debut an approach to exploit this gradient as a highly sensitive ruler to determine the topology, immersion depth, and location of a membrane associating protein, including the segments residing well above the membrane surface, that are otherwise difficult to resolve. This study demonstrates a potential of a broadly applicable approach for the structure–dynamics–function study of membrane proteins, membrane systems, and beyond.

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