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Molecular Motions in Functional Self-Assembled Nanostructures
Int. J. Mol. Sci. 2013, 14(2), 2484-2501; doi:10.3390/ijms14022484
Review

S-Layer Protein Self-Assembly

* ,
 and
Department of Nanobiotechnology, Institute for Biophysics, University of Natural Resources and Life Science, Vienna, Muthgasse 11, Vienna 1190, Austria
* Author to whom correspondence should be addressed.
Received: 14 December 2012 / Revised: 14 January 2013 / Accepted: 16 January 2013 / Published: 25 January 2013
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
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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.
Keywords: S-layer; self-assembly; fusion protein; surface functionalization; nanobiotechnology S-layer; self-assembly; fusion protein; surface functionalization; nanobiotechnology
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Pum, D.; Toca-Herrera, J.L.; Sleytr, U.B. S-Layer Protein Self-Assembly. Int. J. Mol. Sci. 2013, 14, 2484-2501.

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