Self-assembled bionanostructures: proteins following the lead of DNA nanostructures

Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to...
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Autor*in:	Gradišar, Helena [verfasserIn] Jerala, Roman

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2014

Schlagwörter:	Self-assembly Protein nanostructures DNA nanostructures Protein origami

Anmerkung:	© Gradišar and Jerala; licensee BioMed Central Ltd. 2014

Übergeordnetes Werk:	Enthalten in: Journal of nanobiotechnology - London : Biomed Central, 2003, 12(2014), 1 vom: 03. Feb.
Übergeordnetes Werk:	volume:12 ; year:2014 ; number:1 ; day:03 ; month:02

Links:	Volltext

DOI / URN:	10.1186/1477-3155-12-4

Katalog-ID:	SPR029456517

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allfields	10.1186/1477-3155-12-4 doi (DE-627)SPR029456517 (SPR)1477-3155-12-4-e DE-627 ger DE-627 rakwb eng Gradišar, Helena verfasserin aut Self-assembled bionanostructures: proteins following the lead of DNA nanostructures 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Gradišar and Jerala; licensee BioMed Central Ltd. 2014 Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213 Jerala, Roman aut Enthalten in Journal of nanobiotechnology London : Biomed Central, 2003 12(2014), 1 vom: 03. Feb. (DE-627)362770328 (DE-600)2100022-0 1477-3155 nnns volume:12 year:2014 number:1 day:03 month:02 https://dx.doi.org/10.1186/1477-3155-12-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2014 1 03 02
spelling	10.1186/1477-3155-12-4 doi (DE-627)SPR029456517 (SPR)1477-3155-12-4-e DE-627 ger DE-627 rakwb eng Gradišar, Helena verfasserin aut Self-assembled bionanostructures: proteins following the lead of DNA nanostructures 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Gradišar and Jerala; licensee BioMed Central Ltd. 2014 Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213 Jerala, Roman aut Enthalten in Journal of nanobiotechnology London : Biomed Central, 2003 12(2014), 1 vom: 03. Feb. (DE-627)362770328 (DE-600)2100022-0 1477-3155 nnns volume:12 year:2014 number:1 day:03 month:02 https://dx.doi.org/10.1186/1477-3155-12-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2014 1 03 02
allfields_unstemmed	10.1186/1477-3155-12-4 doi (DE-627)SPR029456517 (SPR)1477-3155-12-4-e DE-627 ger DE-627 rakwb eng Gradišar, Helena verfasserin aut Self-assembled bionanostructures: proteins following the lead of DNA nanostructures 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Gradišar and Jerala; licensee BioMed Central Ltd. 2014 Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213 Jerala, Roman aut Enthalten in Journal of nanobiotechnology London : Biomed Central, 2003 12(2014), 1 vom: 03. Feb. (DE-627)362770328 (DE-600)2100022-0 1477-3155 nnns volume:12 year:2014 number:1 day:03 month:02 https://dx.doi.org/10.1186/1477-3155-12-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2014 1 03 02
allfieldsGer	10.1186/1477-3155-12-4 doi (DE-627)SPR029456517 (SPR)1477-3155-12-4-e DE-627 ger DE-627 rakwb eng Gradišar, Helena verfasserin aut Self-assembled bionanostructures: proteins following the lead of DNA nanostructures 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Gradišar and Jerala; licensee BioMed Central Ltd. 2014 Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213 Jerala, Roman aut Enthalten in Journal of nanobiotechnology London : Biomed Central, 2003 12(2014), 1 vom: 03. Feb. (DE-627)362770328 (DE-600)2100022-0 1477-3155 nnns volume:12 year:2014 number:1 day:03 month:02 https://dx.doi.org/10.1186/1477-3155-12-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2014 1 03 02
allfieldsSound	10.1186/1477-3155-12-4 doi (DE-627)SPR029456517 (SPR)1477-3155-12-4-e DE-627 ger DE-627 rakwb eng Gradišar, Helena verfasserin aut Self-assembled bionanostructures: proteins following the lead of DNA nanostructures 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Gradišar and Jerala; licensee BioMed Central Ltd. 2014 Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213 Jerala, Roman aut Enthalten in Journal of nanobiotechnology London : Biomed Central, 2003 12(2014), 1 vom: 03. Feb. (DE-627)362770328 (DE-600)2100022-0 1477-3155 nnns volume:12 year:2014 number:1 day:03 month:02 https://dx.doi.org/10.1186/1477-3155-12-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2014 1 03 02
language	English
source	Enthalten in Journal of nanobiotechnology 12(2014), 1 vom: 03. Feb. volume:12 year:2014 number:1 day:03 month:02
sourceStr	Enthalten in Journal of nanobiotechnology 12(2014), 1 vom: 03. Feb. volume:12 year:2014 number:1 day:03 month:02
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topic_facet	Self-assembly Protein nanostructures DNA nanostructures Protein origami
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container_title	Journal of nanobiotechnology
authorswithroles_txt_mv	Gradišar, Helena @@aut@@ Jerala, Roman @@aut@@
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author	Gradišar, Helena
spellingShingle	Gradišar, Helena misc Self-assembly misc Protein nanostructures misc DNA nanostructures misc Protein origami Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
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topic_title	Self-assembled bionanostructures: proteins following the lead of DNA nanostructures Self-assembly (dpeaa)DE-He213 Protein nanostructures (dpeaa)DE-He213 DNA nanostructures (dpeaa)DE-He213 Protein origami (dpeaa)DE-He213
topic	misc Self-assembly misc Protein nanostructures misc DNA nanostructures misc Protein origami
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title	Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
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title_full	Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
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author_browse	Gradišar, Helena Jerala, Roman
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title_sort	self-assembled bionanostructures: proteins following the lead of dna nanostructures
title_auth	Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
abstract	Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. © Gradišar and Jerala; licensee BioMed Central Ltd. 2014
abstractGer	Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. © Gradišar and Jerala; licensee BioMed Central Ltd. 2014
abstract_unstemmed	Abstract Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. © Gradišar and Jerala; licensee BioMed Central Ltd. 2014
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title_short	Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
url	https://dx.doi.org/10.1186/1477-3155-12-4
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Self-assembled bionanostructures: proteins following the lead of DNA nanostructures

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