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Int. J. Mol. Sci. 2013, 14(2), 2484-2501; doi:10.3390/ijms14022484

S-Layer Protein Self-Assembly

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Received: 14 December 2012; in revised form: 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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

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

AMA Style

Pum D, Toca-Herrera JL, Sleytr UB. S-Layer Protein Self-Assembly. International Journal of Molecular Sciences. 2013; 14(2):2484-2501.

Chicago/Turabian Style

Pum, Dietmar; Toca-Herrera, Jose L.; Sleytr, Uwe B. 2013. "S-Layer Protein Self-Assembly." Int. J. Mol. Sci. 14, no. 2: 2484-2501.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert