Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.
Identifieur interne : 000919 ( PubMed/Curation ); précédent : 000918; suivant : 000920Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.
Auteurs : Naoya Kobayashi [Japon] ; Kouichi Inano ; Kenji Sasahara ; Takaaki Sato [Japon] ; Keisuke Miyazawa [Japon] ; Takeshi Fukuma [Japon] ; Michael H. Hecht [États-Unis] ; Chihong Song [Japon] ; Kazuyoshi Murata [Japon] ; Ryoichi Arai [Japon]Source :
- ACS synthetic biology [ 2161-5063 ] ; 2018.
Descripteurs français
- KwdFr :
- Chromatographie sur gel, Diffraction des rayons X, Diffusion aux petits angles, Dénaturation des protéines, Escherichia coli (génétique), Ingénierie des protéines (), Microscopie à force atomique, Microscopie électronique à transmission, Nanostructures (), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Repliement des protéines.
- MESH :
- génétique : Escherichia coli, Protéines recombinantes.
- métabolisme : Protéines recombinantes.
- Chromatographie sur gel, Diffraction des rayons X, Diffusion aux petits angles, Dénaturation des protéines, Ingénierie des protéines, Microscopie à force atomique, Microscopie électronique à transmission, Nanostructures, Protéines recombinantes, Repliement des protéines.
English descriptors
- KwdEn :
- Chromatography, Gel, Escherichia coli (genetics), Microscopy, Atomic Force, Microscopy, Electron, Transmission, Nanostructures (chemistry), Protein Denaturation, Protein Engineering (methods), Protein Refolding, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Scattering, Small Angle, X-Ray Diffraction.
- MESH :
- chemical , chemistry : Recombinant Proteins.
- chemistry : Nanostructures.
- genetics : Escherichia coli, Recombinant Proteins.
- chemical , metabolism : Recombinant Proteins.
- methods : Protein Engineering.
- Chromatography, Gel, Microscopy, Atomic Force, Microscopy, Electron, Transmission, Protein Denaturation, Protein Refolding, Scattering, Small Angle, X-Ray Diffraction.
Abstract
The design of novel proteins that self-assemble into supramolecular complexes is important for development in nanobiotechnology and synthetic biology. Recently, we designed and created a protein nanobuilding block (PN-Block), WA20-foldon, by fusing an intermolecularly folded dimeric de novo WA20 protein and a trimeric foldon domain of T4 phage fibritin (Kobayashi et al., J. Am. Chem. Soc. 2015, 137, 11285). WA20-foldon formed several types of self-assembling nanoarchitectures in multiples of 6-mers, including a barrel-like hexamer and a tetrahedron-like dodecamer. In this study, to construct chain-like polymeric nanostructures, we designed de novo extender protein nanobuilding blocks (ePN-Blocks) by tandemly fusing two de novo binary-patterned WA20 proteins with various linkers. The ePN-Blocks with long helical linkers or flexible linkers were expressed in soluble fractions of Escherichia coli, and the purified ePN-Blocks were analyzed by native PAGE, size exclusion chromatography-multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS), and transmission electron microscopy. These results suggest formation of various structural homo-oligomers. Subsequently, we reconstructed hetero-oligomeric complexes from extender and stopper PN-Blocks by denaturation and refolding. The present SEC-MALS and SAXS analyses show that extender and stopper PN-Block (esPN-Block) heterocomplexes formed different types of extended chain-like conformations depending on their linker types. Moreover, atomic force microscopy imaging in liquid suggests that the esPN-Block heterocomplexes with metal ions further self-assembled into supramolecular nanostructures on mica surfaces. Taken together, the present data demonstrate that the design and construction of self-assembling PN-Blocks using de novo proteins is a useful strategy for building polymeric nanoarchitectures of supramolecular protein complexes.
DOI: 10.1021/acssynbio.8b00007
PubMed: 29690759
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type="doi">10.1021/acssynbio.8b00007</idno><idno type="wicri:Area/PubMed/Corpus">000919</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000919</idno><idno type="wicri:Area/PubMed/Curation">000919</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000919</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.</title><author><name sortKey="Kobayashi, Naoya" sort="Kobayashi, Naoya" uniqKey="Kobayashi N" first="Naoya" last="Kobayashi">Naoya Kobayashi</name><affiliation wicri:level="1"><nlm:affiliation>Exploratory Research Center on Life and Living Systems , National Institutes of Natural Sciences , Okazaki , Aichi 444-8787 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Exploratory Research Center on Life and Living Systems , National Institutes of Natural Sciences , Okazaki , Aichi 444-8787 </wicri:regionArea></affiliation></author><author><name sortKey="Inano, Kouichi" sort="Inano, Kouichi" uniqKey="Inano K" first="Kouichi" last="Inano">Kouichi Inano</name></author><author><name sortKey="Sasahara, Kenji" sort="Sasahara, Kenji" uniqKey="Sasahara K" first="Kenji" last="Sasahara">Kenji Sasahara</name></author><author><name sortKey="Sato, Takaaki" sort="Sato, Takaaki" uniqKey="Sato T" first="Takaaki" last="Sato">Takaaki Sato</name><affiliation wicri:level="1"><nlm:affiliation>Center for Energy and Environmental Science , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Nagano , Nagano 380-8553 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Center for Energy and Environmental Science , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Nagano , Nagano 380-8553 </wicri:regionArea></affiliation></author><author><name sortKey="Miyazawa, Keisuke" sort="Miyazawa, Keisuke" uniqKey="Miyazawa K" first="Keisuke" last="Miyazawa">Keisuke Miyazawa</name><affiliation wicri:level="1"><nlm:affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 </wicri:regionArea></affiliation></author><author><name sortKey="Fukuma, Takeshi" sort="Fukuma, Takeshi" uniqKey="Fukuma T" first="Takeshi" last="Fukuma">Takeshi Fukuma</name><affiliation wicri:level="1"><nlm:affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 </wicri:regionArea></affiliation></author><author><name sortKey="Hecht, Michael H" sort="Hecht, Michael H" uniqKey="Hecht M" first="Michael H" last="Hecht">Michael H. Hecht</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry , Princeton University , Princeton , New Jersey 08544 , United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry , Princeton University , Princeton , New Jersey 08544 </wicri:regionArea></affiliation></author><author><name sortKey="Song, Chihong" sort="Song, Chihong" uniqKey="Song C" first="Chihong" last="Song">Chihong Song</name><affiliation wicri:level="1"><nlm:affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 </wicri:regionArea></affiliation></author><author><name sortKey="Murata, Kazuyoshi" sort="Murata, Kazuyoshi" uniqKey="Murata K" first="Kazuyoshi" last="Murata">Kazuyoshi Murata</name><affiliation wicri:level="1"><nlm:affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 </wicri:regionArea></affiliation></author><author><name sortKey="Arai, Ryoichi" sort="Arai, Ryoichi" uniqKey="Arai R" first="Ryoichi" last="Arai">Ryoichi Arai</name><affiliation wicri:level="1"><nlm:affiliation>Division of Structural and Synthetic Biology , RIKEN Center for Life Science Technologies , Tsurumi , Yokohama 230-0045 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Structural and Synthetic Biology , RIKEN Center for Life Science Technologies , Tsurumi , Yokohama 230-0045 </wicri:regionArea></affiliation></author></analytic><series><title level="j">ACS synthetic biology</title><idno type="eISSN">2161-5063</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Gel</term><term>Escherichia coli (genetics)</term><term>Microscopy, Atomic Force</term><term>Microscopy, Electron, Transmission</term><term>Nanostructures (chemistry)</term><term>Protein Denaturation</term><term>Protein Engineering (methods)</term><term>Protein Refolding</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Scattering, Small Angle</term><term>X-Ray Diffraction</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Dénaturation des protéines</term><term>Escherichia coli (génétique)</term><term>Ingénierie des protéines ()</term><term>Microscopie à force atomique</term><term>Microscopie électronique à transmission</term><term>Nanostructures ()</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Repliement des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Engineering</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Microscopy, Atomic Force</term><term>Microscopy, Electron, Transmission</term><term>Protein Denaturation</term><term>Protein Refolding</term><term>Scattering, Small Angle</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Dénaturation des protéines</term><term>Ingénierie des protéines</term><term>Microscopie à force atomique</term><term>Microscopie électronique à transmission</term><term>Nanostructures</term><term>Protéines recombinantes</term><term>Repliement des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The design of novel proteins that self-assemble into supramolecular complexes is important for development in nanobiotechnology and synthetic biology. Recently, we designed and created a protein nanobuilding block (PN-Block), WA20-foldon, by fusing an intermolecularly folded dimeric de novo WA20 protein and a trimeric foldon domain of T4 phage fibritin (Kobayashi et al., J. Am. Chem. Soc. 2015, 137, 11285). WA20-foldon formed several types of self-assembling nanoarchitectures in multiples of 6-mers, including a barrel-like hexamer and a tetrahedron-like dodecamer. In this study, to construct chain-like polymeric nanostructures, we designed de novo extender protein nanobuilding blocks (ePN-Blocks) by tandemly fusing two de novo binary-patterned WA20 proteins with various linkers. The ePN-Blocks with long helical linkers or flexible linkers were expressed in soluble fractions of Escherichia coli, and the purified ePN-Blocks were analyzed by native PAGE, size exclusion chromatography-multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS), and transmission electron microscopy. These results suggest formation of various structural homo-oligomers. Subsequently, we reconstructed hetero-oligomeric complexes from extender and stopper PN-Blocks by denaturation and refolding. The present SEC-MALS and SAXS analyses show that extender and stopper PN-Block (esPN-Block) heterocomplexes formed different types of extended chain-like conformations depending on their linker types. Moreover, atomic force microscopy imaging in liquid suggests that the esPN-Block heterocomplexes with metal ions further self-assembled into supramolecular nanostructures on mica surfaces. Taken together, the present data demonstrate that the design and construction of self-assembling PN-Blocks using de novo proteins is a useful strategy for building polymeric nanoarchitectures of supramolecular protein complexes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29690759</PMID><DateCompleted><Year>2019</Year><Month>07</Month><Day>11</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>11</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2161-5063</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>5</Issue><PubDate><Year>2018</Year><Month>05</Month><Day>18</Day></PubDate></JournalIssue><Title>ACS synthetic biology</Title><ISOAbbreviation>ACS Synth Biol</ISOAbbreviation></Journal><ArticleTitle>Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.</ArticleTitle><Pagination><MedlinePgn>1381-1394</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acssynbio.8b00007</ELocationID><Abstract><AbstractText>The design of novel proteins that self-assemble into supramolecular complexes is important for development in nanobiotechnology and synthetic biology. Recently, we designed and created a protein nanobuilding block (PN-Block), WA20-foldon, by fusing an intermolecularly folded dimeric de novo WA20 protein and a trimeric foldon domain of T4 phage fibritin (Kobayashi et al., J. Am. Chem. Soc. 2015, 137, 11285). WA20-foldon formed several types of self-assembling nanoarchitectures in multiples of 6-mers, including a barrel-like hexamer and a tetrahedron-like dodecamer. In this study, to construct chain-like polymeric nanostructures, we designed de novo extender protein nanobuilding blocks (ePN-Blocks) by tandemly fusing two de novo binary-patterned WA20 proteins with various linkers. The ePN-Blocks with long helical linkers or flexible linkers were expressed in soluble fractions of Escherichia coli, and the purified ePN-Blocks were analyzed by native PAGE, size exclusion chromatography-multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS), and transmission electron microscopy. These results suggest formation of various structural homo-oligomers. Subsequently, we reconstructed hetero-oligomeric complexes from extender and stopper PN-Blocks by denaturation and refolding. The present SEC-MALS and SAXS analyses show that extender and stopper PN-Block (esPN-Block) heterocomplexes formed different types of extended chain-like conformations depending on their linker types. Moreover, atomic force microscopy imaging in liquid suggests that the esPN-Block heterocomplexes with metal ions further self-assembled into supramolecular nanostructures on mica surfaces. Taken together, the present data demonstrate that the design and construction of self-assembling PN-Blocks using de novo proteins is a useful strategy for building polymeric nanoarchitectures of supramolecular protein complexes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kobayashi</LastName><ForeName>Naoya</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Exploratory Research Center on Life and Living Systems , National Institutes of Natural Sciences , Okazaki , Aichi 444-8787 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Inano</LastName><ForeName>Kouichi</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sasahara</LastName><ForeName>Kenji</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Takaaki</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0002-3455-4349</Identifier><AffiliationInfo><Affiliation>Center for Energy and Environmental Science , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Nagano , Nagano 380-8553 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Miyazawa</LastName><ForeName>Keisuke</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fukuma</LastName><ForeName>Takeshi</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0001-8971-6002</Identifier><AffiliationInfo><Affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hecht</LastName><ForeName>Michael H</ForeName><Initials>MH</Initials><AffiliationInfo><Affiliation>Department of Chemistry , Princeton University , Princeton , New Jersey 08544 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Chihong</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Murata</LastName><ForeName>Kazuyoshi</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Arai</LastName><ForeName>Ryoichi</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0001-5606-8483</Identifier><AffiliationInfo><Affiliation>Division of Structural and Synthetic Biology , RIKEN Center for Life Science Technologies , Tsurumi , Yokohama 230-0045 , Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institute for Biomedical Sciences , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Matsumoto , Nagano 390-8621 , Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Supramolecular Complexes , Research Center for Fungal and Microbial Dynamism, Shinshu University , Minamiminowa , Nagano 399-4598 , Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>ACS Synth Biol</MedlineTA><NlmUniqueID>101575075</NlmUniqueID><ISSNLinking>2161-5063</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018625" MajorTopicYN="N">Microscopy, Atomic Force</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049329" MajorTopicYN="N">Nanostructures</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058849" MajorTopicYN="N">Protein Refolding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053838" MajorTopicYN="N">Scattering, Small Angle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">de novo protein</Keyword><Keyword MajorTopicYN="Y">nanostructure</Keyword><Keyword MajorTopicYN="Y">protein engineering</Keyword><Keyword MajorTopicYN="Y">protein nanobuilding block</Keyword><Keyword MajorTopicYN="Y">protein-based supramolecular polymers</Keyword><Keyword MajorTopicYN="Y">self-assembly</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>7</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29690759</ArticleId><ArticleId IdType="doi">10.1021/acssynbio.8b00007</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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|area= MersV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:29690759
|texte= Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:29690759" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |