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      S-Layer Protein Self-Assembly

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          Abstract

          Crystalline S(urface)-layers are the most commonly observed cell surface structures in prokaryotic organisms (bacteria and archaea). S-layers are highly porous protein meshworks with unit cell sizes in the range of 3 to 30 nm, and thicknesses of ~10 nm. One of the key features of S-layer proteins is their intrinsic capability to form self-assembled mono- or double layers in solution, and at interfaces. Basic research on S-layer proteins laid foundation to make use of the unique self-assembly properties of native and, in particular, genetically functionalized S-layer protein lattices, in a broad range of applications in the life and non-life sciences. This contribution briefly summarizes the knowledge about structure, genetics, chemistry, morphogenesis, and function of S-layer proteins and pays particular attention to the self-assembly in solution, and at differently functionalized solid supports.

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          S-Layer proteins.

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            Crystalline bacterial cell surface layers (s layers): from supramolecular cell structure to biomimetics and nanotechnology.

            An astonishingly broad application potential in biotechnology, biomimetics, and nanotechnology is revealed by studies on the structure, chemistry, biosynthesis, genetics, self-assembly, and function of supramolecular surface layers (S layers). These are monomolecular, crystalline assemblies of protein or glycoprotein subunits and represent one of the most commonly observed surface structures of prokaryotic cell envelopes (see schematic representation of an archaebacterial cell envelope). Copyright © 1999 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.
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              Bacterial S-layers.

              S-layers are produced by the self assembly of proteinaceous subunits on the surfaces of prokaryotes, so that planar, monomolecular-thick crystalline lattices are formed. Some archaeal and eubacterial S-layer proteins are glycosylated. These lattices typically have center-to-center spacings of less than 25 nm, which makes them attractive for biomimetic or nanotechnological applications.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                Molecular Diversity Preservation International (MDPI)
                1422-0067
                2013
                25 January 2013
                : 14
                : 2
                : 2484-2501
                Affiliations
                Department of Nanobiotechnology, Institute for Biophysics, University of Natural Resources and Life Science, Vienna, Muthgasse 11, Vienna 1190, Austria; E-Mails: jose.toca-herrera@ 123456boku.ac.at (J.L.T.-H); uwe.sleytr@ 123456boku.ac.at (U.B.S.)
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: dietmar.pum@ 123456boku.ac.at ; Tel.: +43-1-47654 (ext. 2205); Fax: +43-1-4789112.
                Article
                ijms-14-02484
                10.3390/ijms14022484
                3587997
                23354479
                b0998181-98b9-4ef9-8d42-2648937d8b94
                © 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 14 December 2012
                : 14 January 2013
                : 16 January 2013
                Categories
                Review

                Molecular biology
                s-layer,self-assembly,fusion protein,surface functionalization,nanobiotechnology
                Molecular biology
                s-layer, self-assembly, fusion protein, surface functionalization, nanobiotechnology

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