The self-organizing properties of squid reflectin protein
Reflectins, a recently identified protein family that is enriched in aromatic and sulphur-containing amino acids, are used by certain cephalopods to manage and manipulate incident light in their environment. These proteins are the predominant constituent of nanoscaled photonic structures that functi...
Gespeichert in:
Veröffentlicht in: | Nature materials 2007-07, Vol.6 (7), p.533-538 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 538 |
---|---|
container_issue | 7 |
container_start_page | 533 |
container_title | Nature materials |
container_volume | 6 |
creator | Naik, Rajesh R Kramer, Ryan M Crookes-Goodson, Wendy J |
description | Reflectins, a recently identified protein family that is enriched in aromatic and sulphur-containing amino acids, are used by certain cephalopods to manage and manipulate incident light in their environment. These proteins are the predominant constituent of nanoscaled photonic structures that function in static and adaptive colouration, extending visual performance and intra-species communication. Our investigation into recombinantly expressed reflectin has revealed unanticipated self-assembling and behavioural properties, and we demonstrate that reflectin can be easily processed into thin films, photonic grating structures and fibres. Our findings represent a key step in our understanding of the property–function relationships of this unique family of reflective proteins. |
doi_str_mv | 10.1038/nmat1930 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70662047</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70662047</sourcerecordid><originalsourceid>FETCH-LOGICAL-c496t-944ca6e6d6a302ebf4f6550ee18cb436acb1865a758c8e63606df471dd6cb8833</originalsourceid><addsrcrecordid>eNqF0E1Lw0AQBuBFFKtV8BdI8CB6iM5-ZJIcpfgFBS_1HDabSU1JN-1uctBfb0pjC4J42oV5eId5GbvgcMdBJvd2qVueSjhgJ1zFGCpEOBz-nAsxYqfeLwAEjyI8ZiMeRwpB4glLZx8UeKrLsHFzbauvys6DlWtW5NqKfNCUgV93VRE4KmsybWU305Yqe8aOSl17Oh_eMXt_epxNXsLp2_Pr5GEaGpViG6ZKGY2EBWoJgvJSlRhFQMQTkyuJ2uQ8wUjHUWISQomARaliXhRo8iSRcsyut7n93nVHvs2WlTdU19pS0_ksBkQBKv4XShRJCoA9vPoFF03nbH9EJoSIEQDSHt1skXGN9_312cpVS-0-Mw7ZpvTsp_SeXg55Xb6kYg-HlntwuwW-H9k5uf3Cv8OsbjtHu7Ad-Ab7JJSU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>222760009</pqid></control><display><type>article</type><title>The self-organizing properties of squid reflectin protein</title><source>MEDLINE</source><source>Nature</source><source>Alma/SFX Local Collection</source><creator>Naik, Rajesh R ; Kramer, Ryan M ; Crookes-Goodson, Wendy J</creator><creatorcontrib>Naik, Rajesh R ; Kramer, Ryan M ; Crookes-Goodson, Wendy J</creatorcontrib><description>Reflectins, a recently identified protein family that is enriched in aromatic and sulphur-containing amino acids, are used by certain cephalopods to manage and manipulate incident light in their environment. These proteins are the predominant constituent of nanoscaled photonic structures that function in static and adaptive colouration, extending visual performance and intra-species communication. Our investigation into recombinantly expressed reflectin has revealed unanticipated self-assembling and behavioural properties, and we demonstrate that reflectin can be easily processed into thin films, photonic grating structures and fibres. Our findings represent a key step in our understanding of the property–function relationships of this unique family of reflective proteins.</description><identifier>ISSN: 1476-1122</identifier><identifier>EISSN: 1476-4660</identifier><identifier>DOI: 10.1038/nmat1930</identifier><identifier>PMID: 17546036</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino acids ; Animals ; Biomaterials ; Chemistry and Materials Science ; Condensed Matter Physics ; Decapodiformes ; Fibers ; Gene Expression Regulation ; Light ; Materials Science ; Membranes, Artificial ; Microscopy, Electron ; Nanotechnology ; Optical and Electronic Materials ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Structure-Activity Relationship ; Surface Properties ; Thin films</subject><ispartof>Nature materials, 2007-07, Vol.6 (7), p.533-538</ispartof><rights>Springer Nature Limited 2007</rights><rights>Copyright Nature Publishing Group Jul 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c496t-944ca6e6d6a302ebf4f6550ee18cb436acb1865a758c8e63606df471dd6cb8833</citedby><cites>FETCH-LOGICAL-c496t-944ca6e6d6a302ebf4f6550ee18cb436acb1865a758c8e63606df471dd6cb8833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17546036$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Naik, Rajesh R</creatorcontrib><creatorcontrib>Kramer, Ryan M</creatorcontrib><creatorcontrib>Crookes-Goodson, Wendy J</creatorcontrib><title>The self-organizing properties of squid reflectin protein</title><title>Nature materials</title><addtitle>Nature Mater</addtitle><addtitle>Nat Mater</addtitle><description>Reflectins, a recently identified protein family that is enriched in aromatic and sulphur-containing amino acids, are used by certain cephalopods to manage and manipulate incident light in their environment. These proteins are the predominant constituent of nanoscaled photonic structures that function in static and adaptive colouration, extending visual performance and intra-species communication. Our investigation into recombinantly expressed reflectin has revealed unanticipated self-assembling and behavioural properties, and we demonstrate that reflectin can be easily processed into thin films, photonic grating structures and fibres. Our findings represent a key step in our understanding of the property–function relationships of this unique family of reflective proteins.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Biomaterials</subject><subject>Chemistry and Materials Science</subject><subject>Condensed Matter Physics</subject><subject>Decapodiformes</subject><subject>Fibers</subject><subject>Gene Expression Regulation</subject><subject>Light</subject><subject>Materials Science</subject><subject>Membranes, Artificial</subject><subject>Microscopy, Electron</subject><subject>Nanotechnology</subject><subject>Optical and Electronic Materials</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Structure-Activity Relationship</subject><subject>Surface Properties</subject><subject>Thin films</subject><issn>1476-1122</issn><issn>1476-4660</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0E1Lw0AQBuBFFKtV8BdI8CB6iM5-ZJIcpfgFBS_1HDabSU1JN-1uctBfb0pjC4J42oV5eId5GbvgcMdBJvd2qVueSjhgJ1zFGCpEOBz-nAsxYqfeLwAEjyI8ZiMeRwpB4glLZx8UeKrLsHFzbauvys6DlWtW5NqKfNCUgV93VRE4KmsybWU305Yqe8aOSl17Oh_eMXt_epxNXsLp2_Pr5GEaGpViG6ZKGY2EBWoJgvJSlRhFQMQTkyuJ2uQ8wUjHUWISQomARaliXhRo8iSRcsyut7n93nVHvs2WlTdU19pS0_ksBkQBKv4XShRJCoA9vPoFF03nbH9EJoSIEQDSHt1skXGN9_312cpVS-0-Mw7ZpvTsp_SeXg55Xb6kYg-HlntwuwW-H9k5uf3Cv8OsbjtHu7Ad-Ab7JJSU</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Naik, Rajesh R</creator><creator>Kramer, Ryan M</creator><creator>Crookes-Goodson, Wendy J</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7SR</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>K9.</scope><scope>KB.</scope><scope>L6V</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7S</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7U5</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20070701</creationdate><title>The self-organizing properties of squid reflectin protein</title><author>Naik, Rajesh R ; Kramer, Ryan M ; Crookes-Goodson, Wendy J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c496t-944ca6e6d6a302ebf4f6550ee18cb436acb1865a758c8e63606df471dd6cb8833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Biomaterials</topic><topic>Chemistry and Materials Science</topic><topic>Condensed Matter Physics</topic><topic>Decapodiformes</topic><topic>Fibers</topic><topic>Gene Expression Regulation</topic><topic>Light</topic><topic>Materials Science</topic><topic>Membranes, Artificial</topic><topic>Microscopy, Electron</topic><topic>Nanotechnology</topic><topic>Optical and Electronic Materials</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Structure-Activity Relationship</topic><topic>Surface Properties</topic><topic>Thin films</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Naik, Rajesh R</creatorcontrib><creatorcontrib>Kramer, Ryan M</creatorcontrib><creatorcontrib>Crookes-Goodson, Wendy J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Engineered Materials Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Engineering Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Engineering Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Nature materials</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Naik, Rajesh R</au><au>Kramer, Ryan M</au><au>Crookes-Goodson, Wendy J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The self-organizing properties of squid reflectin protein</atitle><jtitle>Nature materials</jtitle><stitle>Nature Mater</stitle><addtitle>Nat Mater</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>6</volume><issue>7</issue><spage>533</spage><epage>538</epage><pages>533-538</pages><issn>1476-1122</issn><eissn>1476-4660</eissn><abstract>Reflectins, a recently identified protein family that is enriched in aromatic and sulphur-containing amino acids, are used by certain cephalopods to manage and manipulate incident light in their environment. These proteins are the predominant constituent of nanoscaled photonic structures that function in static and adaptive colouration, extending visual performance and intra-species communication. Our investigation into recombinantly expressed reflectin has revealed unanticipated self-assembling and behavioural properties, and we demonstrate that reflectin can be easily processed into thin films, photonic grating structures and fibres. Our findings represent a key step in our understanding of the property–function relationships of this unique family of reflective proteins.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>17546036</pmid><doi>10.1038/nmat1930</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1476-1122 |
ispartof | Nature materials, 2007-07, Vol.6 (7), p.533-538 |
issn | 1476-1122 1476-4660 |
language | eng |
recordid | cdi_proquest_miscellaneous_70662047 |
source | MEDLINE; Nature; Alma/SFX Local Collection |
subjects | Amino acids Animals Biomaterials Chemistry and Materials Science Condensed Matter Physics Decapodiformes Fibers Gene Expression Regulation Light Materials Science Membranes, Artificial Microscopy, Electron Nanotechnology Optical and Electronic Materials Proteins Proteins - chemistry Proteins - metabolism Structure-Activity Relationship Surface Properties Thin films |
title | The self-organizing properties of squid reflectin protein |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T09%3A38%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20self-organizing%20properties%20of%20squid%20reflectin%20protein&rft.jtitle=Nature%20materials&rft.au=Naik,%20Rajesh%20R&rft.date=2007-07-01&rft.volume=6&rft.issue=7&rft.spage=533&rft.epage=538&rft.pages=533-538&rft.issn=1476-1122&rft.eissn=1476-4660&rft_id=info:doi/10.1038/nmat1930&rft_dat=%3Cproquest_cross%3E70662047%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=222760009&rft_id=info:pmid/17546036&rfr_iscdi=true |