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S-Layer Protein Self-Assembly
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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587997/ https://www.ncbi.nlm.nih.gov/pubmed/23354479 http://dx.doi.org/10.3390/ijms14022484 |
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author | Pum, Dietmar Toca-Herrera, Jose Luis Sleytr, Uwe B. |
author_facet | Pum, Dietmar Toca-Herrera, Jose Luis Sleytr, Uwe B. |
author_sort | Pum, Dietmar |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3587997 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-35879972013-03-13 S-Layer Protein Self-Assembly Pum, Dietmar Toca-Herrera, Jose Luis Sleytr, Uwe B. Int J Mol Sci Review 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. MDPI 2013-01-25 /pmc/articles/PMC3587997/ /pubmed/23354479 http://dx.doi.org/10.3390/ijms14022484 Text en © 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 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/). |
spellingShingle | Review Pum, Dietmar Toca-Herrera, Jose Luis Sleytr, Uwe B. S-Layer Protein Self-Assembly |
title | S-Layer Protein Self-Assembly |
title_full | S-Layer Protein Self-Assembly |
title_fullStr | S-Layer Protein Self-Assembly |
title_full_unstemmed | S-Layer Protein Self-Assembly |
title_short | S-Layer Protein Self-Assembly |
title_sort | s-layer protein self-assembly |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587997/ https://www.ncbi.nlm.nih.gov/pubmed/23354479 http://dx.doi.org/10.3390/ijms14022484 |
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