Artificial diiron proteins: From structure to function
De novo protein design provides an attractive approach for the construction of models to probe the features required for the function of complex metalloproteins. These minimal models contain the essential elements believed necessary for activity of the protein. In this article, we summarize the desi...
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| Veröffentlicht in: | Biopolymers 2005, Vol.80 (2-3), p.264-278 |
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| container_end_page | 278 |
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| container_issue | 2-3 |
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| container_title | Biopolymers |
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| creator | Calhoun, Jennifer R. Nastri, Flavia Maglio, Ornella Pavone, Vincenzo Lombardi, Angela DeGrado, William F. |
| description | De novo protein design provides an attractive approach for the construction of models to probe the features required for the function of complex metalloproteins. These minimal models contain the essential elements believed necessary for activity of the protein. In this article, we summarize the design, structure determination, and functional properties of a family of artificial diiron proteins. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005 |
| doi_str_mv | 10.1002/bip.20230 |
| format | Article |
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These minimal models contain the essential elements believed necessary for activity of the protein. In this article, we summarize the design, structure determination, and functional properties of a family of artificial diiron proteins. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.20230</identifier><identifier>PMID: 15700297</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Sequence ; Catalytic Domain ; computational protein design ; de novo protein design ; diiron protein ; Dimerization ; Iron - chemistry ; metalloprotein ; Metalloproteins - chemical synthesis ; Metalloproteins - chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Quaternary ; Static Electricity ; structure ; Thermodynamics</subject><ispartof>Biopolymers, 2005, Vol.80 (2-3), p.264-278</ispartof><rights>Copyright © 2005 Wiley Periodicals, Inc.</rights><rights>Copyright 2005 Wiley Periodicals, Inc</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5260-faac4826967d30634e169d7fc71e2730a33f3ebb424d1c6b1ab7ecefec1c7b2c3</citedby><cites>FETCH-LOGICAL-c5260-faac4826967d30634e169d7fc71e2730a33f3ebb424d1c6b1ab7ecefec1c7b2c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.20230$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.20230$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,4025,27928,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15700297$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Calhoun, Jennifer R.</creatorcontrib><creatorcontrib>Nastri, Flavia</creatorcontrib><creatorcontrib>Maglio, Ornella</creatorcontrib><creatorcontrib>Pavone, Vincenzo</creatorcontrib><creatorcontrib>Lombardi, Angela</creatorcontrib><creatorcontrib>DeGrado, William F.</creatorcontrib><title>Artificial diiron proteins: From structure to function</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>De novo protein design provides an attractive approach for the construction of models to probe the features required for the function of complex metalloproteins. These minimal models contain the essential elements believed necessary for activity of the protein. In this article, we summarize the design, structure determination, and functional properties of a family of artificial diiron proteins. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005</description><subject>Amino Acid Sequence</subject><subject>Catalytic Domain</subject><subject>computational protein design</subject><subject>de novo protein design</subject><subject>diiron protein</subject><subject>Dimerization</subject><subject>Iron - chemistry</subject><subject>metalloprotein</subject><subject>Metalloproteins - chemical synthesis</subject><subject>Metalloproteins - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure, Quaternary</subject><subject>Static Electricity</subject><subject>structure</subject><subject>Thermodynamics</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkDtPwzAURi0EoqUw8AdQJhBDyvUjdsIGhZZKFQ-piNFyHEcypEmxEwH_HkMLTCCmu5zv6OogtI9hiAHISW6XQwKEwgbqY8hEDCQlm6gPADymCUl6aMf7RwDGKIZt1MOJCLtM9BE_c60trbaqigprXVNHS9e0xtb-NBq7ZhH51nW67ZyJ2iYqu1q3tql30VapKm_21neA7seX89FVPLuZTEdns1gnhENcKqVZSnjGRUGBU2YwzwpRaoENERQUpSU1ec4IK7DmOVa5MNqURmMtcqLpAB2tvOGp5874Vi6s16aqVG2azkvBkiCHLPsHSQXDacYCefgnyYUQNOUigMcrULvGe2dKuXR2odybxCA_wssQXn6GD-zBWtrlC1P8kOvSAThZAS-2Mm-_m-T59PZLGa8W1rfm9Xuh3FN4kYpEPlxPJLsYzVk6v5MT-g46Z5rd</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>Calhoun, Jennifer R.</creator><creator>Nastri, Flavia</creator><creator>Maglio, Ornella</creator><creator>Pavone, Vincenzo</creator><creator>Lombardi, Angela</creator><creator>DeGrado, William F.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><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>7X8</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7QO</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2005</creationdate><title>Artificial diiron proteins: From structure to function</title><author>Calhoun, Jennifer R. ; Nastri, Flavia ; Maglio, Ornella ; Pavone, Vincenzo ; Lombardi, Angela ; DeGrado, William F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5260-faac4826967d30634e169d7fc71e2730a33f3ebb424d1c6b1ab7ecefec1c7b2c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Catalytic Domain</topic><topic>computational protein design</topic><topic>de novo protein design</topic><topic>diiron protein</topic><topic>Dimerization</topic><topic>Iron - chemistry</topic><topic>metalloprotein</topic><topic>Metalloproteins - chemical synthesis</topic><topic>Metalloproteins - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Structure, Quaternary</topic><topic>Static Electricity</topic><topic>structure</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Calhoun, Jennifer R.</creatorcontrib><creatorcontrib>Nastri, Flavia</creatorcontrib><creatorcontrib>Maglio, Ornella</creatorcontrib><creatorcontrib>Pavone, Vincenzo</creatorcontrib><creatorcontrib>Lombardi, Angela</creatorcontrib><creatorcontrib>DeGrado, William F.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Biotechnology Research Abstracts</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Calhoun, Jennifer R.</au><au>Nastri, Flavia</au><au>Maglio, Ornella</au><au>Pavone, Vincenzo</au><au>Lombardi, Angela</au><au>DeGrado, William F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Artificial diiron proteins: From structure to function</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>2005</date><risdate>2005</risdate><volume>80</volume><issue>2-3</issue><spage>264</spage><epage>278</epage><pages>264-278</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>De novo protein design provides an attractive approach for the construction of models to probe the features required for the function of complex metalloproteins. 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| ispartof | Biopolymers, 2005, Vol.80 (2-3), p.264-278 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library All Journals |
| subjects | Amino Acid Sequence Catalytic Domain computational protein design de novo protein design diiron protein Dimerization Iron - chemistry metalloprotein Metalloproteins - chemical synthesis Metalloproteins - chemistry Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Quaternary Static Electricity structure Thermodynamics |
| title | Artificial diiron proteins: From structure to function |
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