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      High-resolution atomic force microscopy and spectroscopy of native membrane proteins

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      Reports on Progress in Physics

      IOP Publishing

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          Atomic Force Microscope

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            Membrane lipids: where they are and how they behave.

            Throughout the biological world, a 30 A hydrophobic film typically delimits the environments that serve as the margin between life and death for individual cells. Biochemical and biophysical findings have provided a detailed model of the composition and structure of membranes, which includes levels of dynamic organization both across the lipid bilayer (lipid asymmetry) and in the lateral dimension (lipid domains) of membranes. How do cells apply anabolic and catabolic enzymes, translocases and transporters, plus the intrinsic physical phase behaviour of lipids and their interactions with membrane proteins, to create the unique compositions and multiple functionalities of their individual membranes?
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              Lipid rafts as a membrane-organizing principle.

              Cell membranes display a tremendous complexity of lipids and proteins designed to perform the functions cells require. To coordinate these functions, the membrane is able to laterally segregate its constituents. This capability is based on dynamic liquid-liquid immiscibility and underlies the raft concept of membrane subcompartmentalization. Lipid rafts are fluctuating nanoscale assemblies of sphingolipid, cholesterol, and proteins that can be stabilized to coalesce, forming platforms that function in membrane signaling and trafficking. Here we review the evidence for how this principle combines the potential for sphingolipid-cholesterol self-assembly with protein specificity to selectively focus membrane bioactivity.
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                Author and article information

                Journal
                Reports on Progress in Physics
                Rep. Prog. Phys.
                IOP Publishing
                0034-4885
                1361-6633
                August 01 2011
                August 01 2011
                : 74
                : 8
                : 086601
                Article
                10.1088/0034-4885/74/8/086601
                © 2011

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