Acyl carrier protein structural classification and normal mode analysis
All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are...
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Veröffentlicht in: | Protein science 2012-05, Vol.21 (5), p.655-666 |
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description | All acyl carrier protein primary and tertiary structures were gathered into the ThYme database. They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well. |
doi_str_mv | 10.1002/pro.2050 |
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They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. 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They are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuations at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three acyl carrier protein families that lacked any known structures were predicted as well.</description><subject>acyl carrier protein</subject><subject>Acyl Carrier Protein - chemistry</subject><subject>Acyl Carrier Protein - classification</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Avian Proteins - chemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Chickens</subject><subject>Fungal Proteins - chemistry</subject><subject>Humans</subject><subject>Meat processing</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>normal mode analysis</subject><subject>Phylogeny</subject><subject>primary structure</subject><subject>protein family</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>tertiary structure</subject><subject>ThYme</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1LwzAYhYMobk7BXyAFL_SmM19tkxthDJ3CQBEF70KapprRNjNplf57MzeHCl6Fl_PwcMIB4BjBMYIQXyydHWOYwB0wRDTlMePp8y4YQp6imJGUDcCB9wsIIUWY7IMBxiSjLOFDMJuovoqUdM5oFwVPq00T-dZ1qu2cDFElvTelUbI1tolkU0SNdXVIalvocMuq98Yfgr1SVl4fbd4ReLq-epzexPO72e10Mo8VJRmMNS8RxTnRWCLFqcwKihFiHJUJR2lOiiQhqiS4zDXVRRIQKqnUBc5ZgTKMyAhcrr3LLq91oXTThpZi6UwtXS-sNOJ30phX8WLfBaGQ0JQEwdlG4Oxbp30rauOVrirZaNt5wTnhkDNCA3n6h1zYzoX_eoGyNGUUMcwCdb6mlLPeO11uuyAoVuOE24rVOAE9-dl9C36vEYB4DXyYSvf_isT9w92X8BPkPZnJ</recordid><startdate>201205</startdate><enddate>201205</enddate><creator>Cantu, David C.</creator><creator>Forrester, Michael J.</creator><creator>Charov, Katherine</creator><creator>Reilly, Peter J.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley Subscription Services, Inc</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>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201205</creationdate><title>Acyl carrier protein structural classification and normal mode analysis</title><author>Cantu, David C. ; 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subjects | acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - classification Amino Acid Sequence Animals Avian Proteins - chemistry Bacterial Proteins - chemistry Chickens Fungal Proteins - chemistry Humans Meat processing Models, Molecular Molecular Sequence Data normal mode analysis Phylogeny primary structure protein family Protein Structure, Tertiary Proteins Sequence Alignment tertiary structure ThYme |
title | Acyl carrier protein structural classification and normal mode analysis |
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