Prediction of potential thermostable proteins in Xylella fastidiosa
The average protein ( E+ K)/( Q+ H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile, Xylella fastidiosa. Nine prot...
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| Veröffentlicht in: | Journal of theoretical biology 2006-09, Vol.242 (2), p.421-425 |
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| container_issue | 2 |
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| container_title | Journal of theoretical biology |
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| creator | Van der Linden, M.G. Rêgo, T.G. Araújo, D.A.M. Farias, S.T. |
| description | The average protein (
E+
K)/(
Q+
H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile,
Xylella fastidiosa. Nine proteins were chosen to have their three-dimensional structures modeled by homology, using mainly proteins from mesophiles as templates. Resulting models featured a high number of hydrophobic interactions, a property that has been previously associated with thermostability. These results demonstrate the interesting possibility of using the (
E+
K)/(
Q+
H) ratio to find individual thermostable proteins in mesophilic organisms. |
| doi_str_mv | 10.1016/j.jtbi.2006.03.009 |
| format | Article |
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E+
K)/(
Q+
H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile,
Xylella fastidiosa. Nine proteins were chosen to have their three-dimensional structures modeled by homology, using mainly proteins from mesophiles as templates. Resulting models featured a high number of hydrophobic interactions, a property that has been previously associated with thermostability. These results demonstrate the interesting possibility of using the (
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H) ratio to find individual thermostable proteins in mesophilic organisms.</description><identifier>ISSN: 0022-5193</identifier><identifier>EISSN: 1095-8541</identifier><identifier>DOI: 10.1016/j.jtbi.2006.03.009</identifier><identifier>PMID: 16631209</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Bacterial Proteins - chemistry ; Chemical Phenomena ; Chemistry, Physical ; Hot Temperature ; Hydrophobic and Hydrophilic Interactions ; Modeling ; Models, Molecular ; Protein ; Protein Conformation ; Temperature ; Thermostability ; Xylella - chemistry ; Xylella fastidiosa</subject><ispartof>Journal of theoretical biology, 2006-09, Vol.242 (2), p.421-425</ispartof><rights>2006 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-a4e8eb4e9b9770b885c424ac946d8f20f84822a60df614e4db05c9e1622416ed3</citedby><cites>FETCH-LOGICAL-c385t-a4e8eb4e9b9770b885c424ac946d8f20f84822a60df614e4db05c9e1622416ed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jtbi.2006.03.009$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16631209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van der Linden, M.G.</creatorcontrib><creatorcontrib>Rêgo, T.G.</creatorcontrib><creatorcontrib>Araújo, D.A.M.</creatorcontrib><creatorcontrib>Farias, S.T.</creatorcontrib><title>Prediction of potential thermostable proteins in Xylella fastidiosa</title><title>Journal of theoretical biology</title><addtitle>J Theor Biol</addtitle><description>The average protein (
E+
K)/(
Q+
H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile,
Xylella fastidiosa. Nine proteins were chosen to have their three-dimensional structures modeled by homology, using mainly proteins from mesophiles as templates. Resulting models featured a high number of hydrophobic interactions, a property that has been previously associated with thermostability. These results demonstrate the interesting possibility of using the (
E+
K)/(
Q+
H) ratio to find individual thermostable proteins in mesophilic organisms.</description><subject>Bacterial Proteins - chemistry</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Hot Temperature</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Modeling</subject><subject>Models, Molecular</subject><subject>Protein</subject><subject>Protein Conformation</subject><subject>Temperature</subject><subject>Thermostability</subject><subject>Xylella - chemistry</subject><subject>Xylella fastidiosa</subject><issn>0022-5193</issn><issn>1095-8541</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEURYMotlb_gAuZlbsZXzKZNAE3UvyCgi4U3IVM5g2mTGdqkgr992ZowZ2uHjzOvVwOIZcUCgpU3KyKVaxdwQBEAWUBoI7IlIKqcllxekymAIzlFVXlhJyFsIJE8FKckgkVoqQM1JQsXj02zkY39NnQZpshYh-d6bL4iX49hGjqDrONT3_Xh8z12ceuw64zWWtCdI0bgjknJ63pAl4c7oy8P9y_LZ7y5cvj8-JumdtSVjE3HCXWHFWt5nOopawsZ9xYxUUjWwat5JIxI6BpBeXImxoqq5AKxjgV2JQzcr3vTXO-thiiXrtgxzE9DtughZzPK8bkv2AywqnkKoFsD1o_hOCx1Rvv1sbvNAU9OtYrPTrWo2MNpU4GU-jq0L6t19j8Rg5SE3C7BzDJ-HbodbAOe5tEe7RRN4P7q_8Hn4qNWQ</recordid><startdate>20060921</startdate><enddate>20060921</enddate><creator>Van der Linden, M.G.</creator><creator>Rêgo, T.G.</creator><creator>Araújo, D.A.M.</creator><creator>Farias, S.T.</creator><general>Elsevier Ltd</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20060921</creationdate><title>Prediction of potential thermostable proteins in Xylella fastidiosa</title><author>Van der Linden, M.G. ; Rêgo, T.G. ; Araújo, D.A.M. ; Farias, S.T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-a4e8eb4e9b9770b885c424ac946d8f20f84822a60df614e4db05c9e1622416ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Hot Temperature</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Modeling</topic><topic>Models, Molecular</topic><topic>Protein</topic><topic>Protein Conformation</topic><topic>Temperature</topic><topic>Thermostability</topic><topic>Xylella - chemistry</topic><topic>Xylella fastidiosa</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van der Linden, M.G.</creatorcontrib><creatorcontrib>Rêgo, T.G.</creatorcontrib><creatorcontrib>Araújo, D.A.M.</creatorcontrib><creatorcontrib>Farias, S.T.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of theoretical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van der Linden, M.G.</au><au>Rêgo, T.G.</au><au>Araújo, D.A.M.</au><au>Farias, S.T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prediction of potential thermostable proteins in Xylella fastidiosa</atitle><jtitle>Journal of theoretical biology</jtitle><addtitle>J Theor Biol</addtitle><date>2006-09-21</date><risdate>2006</risdate><volume>242</volume><issue>2</issue><spage>421</spage><epage>425</epage><pages>421-425</pages><issn>0022-5193</issn><eissn>1095-8541</eissn><abstract>The average protein (
E+
K)/(
Q+
H) ratio in organisms has already been demonstrated to have a strong correlation with their optimal growth temperature. Employing the Thermo-Search web tool, we used this ratio as a basis to look for thermostable proteins in a mesophile,
Xylella fastidiosa. Nine proteins were chosen to have their three-dimensional structures modeled by homology, using mainly proteins from mesophiles as templates. Resulting models featured a high number of hydrophobic interactions, a property that has been previously associated with thermostability. These results demonstrate the interesting possibility of using the (
E+
K)/(
Q+
H) ratio to find individual thermostable proteins in mesophilic organisms.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>16631209</pmid><doi>10.1016/j.jtbi.2006.03.009</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of theoretical biology, 2006-09, Vol.242 (2), p.421-425 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Bacterial Proteins - chemistry Chemical Phenomena Chemistry, Physical Hot Temperature Hydrophobic and Hydrophilic Interactions Modeling Models, Molecular Protein Protein Conformation Temperature Thermostability Xylella - chemistry Xylella fastidiosa |
| title | Prediction of potential thermostable proteins in Xylella fastidiosa |
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