A thermodynamic study of the 434‐repressor N‐terminal domain and of its covalently linked dimers
The isolated N‐terminal 1–69 domain of the 434‐phage repressor, R69, and its covalently linked (head‐to‐tail and tail‐to‐tail) dimers have been studied by differential scanning microcalorimetry (DSC) and CD. At neutral solvent conditions the R69 domain maintains its native structure, both in isolate...
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| Veröffentlicht in: | European journal of biochemistry 1999-07, Vol.263 (1), p.246-253 |
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| container_title | European journal of biochemistry |
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| creator | Ruiz‐Sanz, Javier Simoncsits, András Törö, Imre Pongor, Sandor Mateo, Pedro L. Filimonov, Vladimir V. |
| description | The isolated N‐terminal 1–69 domain of the 434‐phage repressor, R69, and its covalently linked (head‐to‐tail and tail‐to‐tail) dimers have been studied by differential scanning microcalorimetry (DSC) and CD. At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. At neutral pH and moderate ionic strength, the domains of the dimers behave as two independent units with unfolding parameters similar to those of the isolated domain, which means that linking two R69 domains, either by a long peptide linker or by a designed C‐terminal disulfide bridge, does not induce any cooperation between them. |
| doi_str_mv | 10.1046/j.1432-1327.1999.00491.x |
| format | Article |
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At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. 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At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. At neutral pH and moderate ionic strength, the domains of the dimers behave as two independent units with unfolding parameters similar to those of the isolated domain, which means that linking two R69 domains, either by a long peptide linker or by a designed C‐terminal disulfide bridge, does not induce any cooperation between them.</description><subject>Calorimetry, Differential Scanning</subject><subject>Circular Dichroism</subject><subject>differential scanning microcalorimetry</subject><subject>Dimerization</subject><subject>domain stability</subject><subject>Drug Stability</subject><subject>Hydrogen-Ion Concentration</subject><subject>interdomain interactions</subject><subject>Osmolar Concentration</subject><subject>Phage 434</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>R69 protein</subject><subject>Repressor Proteins - chemistry</subject><subject>thermal stability</subject><subject>Thermodynamics</subject><subject>Viral Proteins</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9O3DAQxq2qCLaUV6h86i1hxvZ640MPFEGphODQ9mw58UT1Nn-2dpaSWx-BZ-RJSAiH3srJY89vvpG_jzGOkCMofbrNUUmRoRSbHI0xOYAymN-_YaulAVK-ZSsAVJkwa33E3qW0BQBt9OaQHU0iwgiEFfNnfPhJse392Lk2VDwNez_yvp6fuZLq8e9DpF2klPrIb6bbMNGhcw33fetCx13nZzwMiVf9nWuoG5qRN6H7RZ770FJM79lB7ZpEJy_nMftxefH9_Cq7vv3y9fzsOquk0ZipQtSShClNLRFFRejWZUGFL0BNv9TKgHHCbHSljK4QoSiUEKUrkaQC0vKYfVx0d7H_vac02DakiprGddTvk9XGSIUa_gviRoFUYj2BxQJWsU8pUm13MbQujhbBzlHYrZ0dt3MUdo7CPkdh76fRDy879mVL_p_BxfsJ-LQAf0JD46uF7eXF529TJZ8AKDyYXA</recordid><startdate>199907</startdate><enddate>199907</enddate><creator>Ruiz‐Sanz, Javier</creator><creator>Simoncsits, András</creator><creator>Törö, Imre</creator><creator>Pongor, Sandor</creator><creator>Mateo, Pedro L.</creator><creator>Filimonov, Vladimir V.</creator><general>Blackwell Science 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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>199907</creationdate><title>A thermodynamic study of the 434‐repressor N‐terminal domain and of its covalently linked dimers</title><author>Ruiz‐Sanz, Javier ; Simoncsits, András ; Törö, Imre ; Pongor, Sandor ; Mateo, Pedro L. ; Filimonov, Vladimir V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3961-482f3e29b9f3112ce1a5b8e8d80419964909a2976c496c11088422bab1e340e63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Calorimetry, Differential Scanning</topic><topic>Circular Dichroism</topic><topic>differential scanning microcalorimetry</topic><topic>Dimerization</topic><topic>domain stability</topic><topic>Drug Stability</topic><topic>Hydrogen-Ion Concentration</topic><topic>interdomain interactions</topic><topic>Osmolar Concentration</topic><topic>Phage 434</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>R69 protein</topic><topic>Repressor Proteins - chemistry</topic><topic>thermal stability</topic><topic>Thermodynamics</topic><topic>Viral Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ruiz‐Sanz, Javier</creatorcontrib><creatorcontrib>Simoncsits, András</creatorcontrib><creatorcontrib>Törö, Imre</creatorcontrib><creatorcontrib>Pongor, Sandor</creatorcontrib><creatorcontrib>Mateo, Pedro L.</creatorcontrib><creatorcontrib>Filimonov, Vladimir V.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ruiz‐Sanz, Javier</au><au>Simoncsits, András</au><au>Törö, Imre</au><au>Pongor, Sandor</au><au>Mateo, Pedro L.</au><au>Filimonov, Vladimir V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A thermodynamic study of the 434‐repressor N‐terminal domain and of its covalently linked dimers</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1999-07</date><risdate>1999</risdate><volume>263</volume><issue>1</issue><spage>246</spage><epage>253</epage><pages>246-253</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The isolated N‐terminal 1–69 domain of the 434‐phage repressor, R69, and its covalently linked (head‐to‐tail and tail‐to‐tail) dimers have been studied by differential scanning microcalorimetry (DSC) and CD. At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. At neutral pH and moderate ionic strength, the domains of the dimers behave as two independent units with unfolding parameters similar to those of the isolated domain, which means that linking two R69 domains, either by a long peptide linker or by a designed C‐terminal disulfide bridge, does not induce any cooperation between them.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10429210</pmid><doi>10.1046/j.1432-1327.1999.00491.x</doi><tpages>8</tpages></addata></record> |
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| subjects | Calorimetry, Differential Scanning Circular Dichroism differential scanning microcalorimetry Dimerization domain stability Drug Stability Hydrogen-Ion Concentration interdomain interactions Osmolar Concentration Phage 434 Protein Conformation Protein Folding R69 protein Repressor Proteins - chemistry thermal stability Thermodynamics Viral Proteins |
| title | A thermodynamic study of the 434‐repressor N‐terminal domain and of its covalently linked dimers |
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