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dc.contributor.author
Mobili, Pablo  
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Serradell, Maria de Los Angeles  
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Mayer, Claudine  
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Arluison, Véronique  
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Gomez Zavaglia, Andrea  
dc.date.available
2016-12-29T20:25:13Z  
dc.date.issued
2013-02  
dc.identifier.citation
Mobili, Pablo; Serradell, Maria de Los Angeles; Mayer, Claudine; Arluison, Véronique; Gomez Zavaglia, Andrea; Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction; SCIENCEDOMAIN International; International Journal of Biochemistry Research & Review; 3; 1; 2-2013; 39-62  
dc.identifier.issn
2231-086X  
dc.identifier.uri
http://hdl.handle.net/11336/10645  
dc.description.abstract
Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered “bottom-up” building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
SCIENCEDOMAIN International  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Protein-Self-Assembly  
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Metal-Ions  
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Biosorption  
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Biomineralization  
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Nanobiotechnology  
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Otras Nanotecnología  
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Nanotecnología  
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INGENIERÍAS Y TECNOLOGÍAS  
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Métodos de Investigación en Bioquímica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
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Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction  
dc.type
info:eu-repo/semantics/article  
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info:ar-repo/semantics/artículo  
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info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-12-12T14:10:00Z  
dc.journal.volume
3  
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1  
dc.journal.pagination
39-62  
dc.journal.pais
Estados Unidos  
dc.description.fil
Fil: Mobili, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones En Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina  
dc.description.fil
Fil: Serradell, Maria de Los Angeles. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina  
dc.description.fil
Fil: Mayer, Claudine. Instituto Pasteur. Departement de Biologie Structurale Et Chimie; Francia. Centre National de la Recherche Scientifique; Francia. Universite Paris Diderot - Paris 7; Francia  
dc.description.fil
Fil: Arluison, Véronique. Commissariat A Energie Atomique; Francia. Laboratoire Jean Perrin; Francia. Universite Paris Diderot - Paris 7; Francia  
dc.description.fil
Fil: Gomez Zavaglia, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones En Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina  
dc.journal.title
International Journal of Biochemistry Research & Review  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.9734/IJBCRR/2013/2431