Folding of the Protein Domain hbSBD
The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, whic...
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 2005-11, Vol.89 (5), p.3353-3361 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3361 |
|---|---|
| container_issue | 5 |
| container_start_page | 3353 |
| container_title | Biophysical journal |
| container_volume | 89 |
| creator | Kouza, Maksim Chang, Chi-Fon Hayryan, Shura Yu, Tsan-hung Li, Mai Suan Huang, Tai-huang Hu, Chin-Kun |
| description | The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, which is well described by the two-state model with the folding temperature TF=317.8±1.95K and the enthalpy change ΔHG=19.67±2.67kcal/mol. The folding is also studied numerically using the off-lattice coarse-grained Go model and the Langevin dynamics. The obtained results, including the population of the native basin, the free-energy landscape as a function of the number of native contacts, and the folding kinetics, also suggest that the hbSBD domain is a two-state folder. These results are consistent with the biological function of hbSBD in branched-chain α-ketoacid dehydrogenase. |
| doi_str_mv | 10.1529/biophysj.105.065151 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1366832</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349505729787</els_id><sourcerecordid>68735910</sourcerecordid><originalsourceid>FETCH-LOGICAL-c484t-8011ed5b2fc07576248238a640db7a9a6eecd14ee02e32506723f5b9a517f6383</originalsourceid><addsrcrecordid>eNp9kdFLHDEQxkOx1NP6FxTKoeDbnjPJJpt9aMFqtYLQQutzyGZnvRx7m2uyd-B_35S7qvXBp4HJb77MfB9jHxBmKHl91viwmj-kxQxBzkBJlPiGTVCWvADQao9NAEAVoqzlPjtIaQGAXAK-Y_uokCvN5YSdXIW-9cP9NHTTcU7THzGM5IfpZVjaXObNzy-X79nbzvaJjnb1kN1dff118a24_X59c3F-W7hSl2OhAZFa2fDOQSUrxUvNhbaqhLapbG0VkWuxJAJOIi-iKi462dRWYtUpocUh-7zVXa2bJbWOhjHa3qyiX9r4YIL15v-Xwc_NfdgYFEppwbPA6U4ght9rSqNZ-uSo7-1AYZ2M0pWQNUIGj1-Ai7COQz7OcJRV9q3EDIkt5GJIKVL3uAmC-ZuA-ZdAbkizTSBPfXx-xNPMzvIMfNoClK3ceIomOU-Do9ZHcqNpg3_1gz_9e5bT</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>215700041</pqid></control><display><type>article</type><title>Folding of the Protein Domain hbSBD</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Cell Press Free Archives</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Kouza, Maksim ; Chang, Chi-Fon ; Hayryan, Shura ; Yu, Tsan-hung ; Li, Mai Suan ; Huang, Tai-huang ; Hu, Chin-Kun</creator><creatorcontrib>Kouza, Maksim ; Chang, Chi-Fon ; Hayryan, Shura ; Yu, Tsan-hung ; Li, Mai Suan ; Huang, Tai-huang ; Hu, Chin-Kun</creatorcontrib><description>The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, which is well described by the two-state model with the folding temperature TF=317.8±1.95K and the enthalpy change ΔHG=19.67±2.67kcal/mol. The folding is also studied numerically using the off-lattice coarse-grained Go model and the Langevin dynamics. The obtained results, including the population of the native basin, the free-energy landscape as a function of the number of native contacts, and the folding kinetics, also suggest that the hbSBD domain is a two-state folder. These results are consistent with the biological function of hbSBD in branched-chain α-ketoacid dehydrogenase.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1529/biophysj.105.065151</identifier><identifier>PMID: 16126825</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) - chemistry ; Animals ; Circular Dichroism ; Enzymes ; Escherichia coli - metabolism ; Hot Temperature ; Kinetics ; Models, Molecular ; Models, Statistical ; Molecular biology ; Molecular structure ; Plasmids - metabolism ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Protein Structure, Tertiary ; Proteins ; Temperature ; Thermodynamics ; Time Factors</subject><ispartof>Biophysical journal, 2005-11, Vol.89 (5), p.3353-3361</ispartof><rights>2005 The Biophysical Society</rights><rights>Copyright Biophysical Society Nov 2005</rights><rights>Copyright © 2005, Biophysical Society 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-8011ed5b2fc07576248238a640db7a9a6eecd14ee02e32506723f5b9a517f6383</citedby><cites>FETCH-LOGICAL-c484t-8011ed5b2fc07576248238a640db7a9a6eecd14ee02e32506723f5b9a517f6383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1366832/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1529/biophysj.105.065151$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3548,27923,27924,45994,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16126825$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kouza, Maksim</creatorcontrib><creatorcontrib>Chang, Chi-Fon</creatorcontrib><creatorcontrib>Hayryan, Shura</creatorcontrib><creatorcontrib>Yu, Tsan-hung</creatorcontrib><creatorcontrib>Li, Mai Suan</creatorcontrib><creatorcontrib>Huang, Tai-huang</creatorcontrib><creatorcontrib>Hu, Chin-Kun</creatorcontrib><title>Folding of the Protein Domain hbSBD</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, which is well described by the two-state model with the folding temperature TF=317.8±1.95K and the enthalpy change ΔHG=19.67±2.67kcal/mol. The folding is also studied numerically using the off-lattice coarse-grained Go model and the Langevin dynamics. The obtained results, including the population of the native basin, the free-energy landscape as a function of the number of native contacts, and the folding kinetics, also suggest that the hbSBD domain is a two-state folder. These results are consistent with the biological function of hbSBD in branched-chain α-ketoacid dehydrogenase.</description><subject>3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) - chemistry</subject><subject>Animals</subject><subject>Circular Dichroism</subject><subject>Enzymes</subject><subject>Escherichia coli - metabolism</subject><subject>Hot Temperature</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Models, Statistical</subject><subject>Molecular biology</subject><subject>Molecular structure</subject><subject>Plasmids - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Temperature</subject><subject>Thermodynamics</subject><subject>Time Factors</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kdFLHDEQxkOx1NP6FxTKoeDbnjPJJpt9aMFqtYLQQutzyGZnvRx7m2uyd-B_35S7qvXBp4HJb77MfB9jHxBmKHl91viwmj-kxQxBzkBJlPiGTVCWvADQao9NAEAVoqzlPjtIaQGAXAK-Y_uokCvN5YSdXIW-9cP9NHTTcU7THzGM5IfpZVjaXObNzy-X79nbzvaJjnb1kN1dff118a24_X59c3F-W7hSl2OhAZFa2fDOQSUrxUvNhbaqhLapbG0VkWuxJAJOIi-iKi462dRWYtUpocUh-7zVXa2bJbWOhjHa3qyiX9r4YIL15v-Xwc_NfdgYFEppwbPA6U4ght9rSqNZ-uSo7-1AYZ2M0pWQNUIGj1-Ai7COQz7OcJRV9q3EDIkt5GJIKVL3uAmC-ZuA-ZdAbkizTSBPfXx-xNPMzvIMfNoClK3ceIomOU-Do9ZHcqNpg3_1gz_9e5bT</recordid><startdate>20051101</startdate><enddate>20051101</enddate><creator>Kouza, Maksim</creator><creator>Chang, Chi-Fon</creator><creator>Hayryan, Shura</creator><creator>Yu, Tsan-hung</creator><creator>Li, Mai Suan</creator><creator>Huang, Tai-huang</creator><creator>Hu, Chin-Kun</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051101</creationdate><title>Folding of the Protein Domain hbSBD</title><author>Kouza, Maksim ; Chang, Chi-Fon ; Hayryan, Shura ; Yu, Tsan-hung ; Li, Mai Suan ; Huang, Tai-huang ; Hu, Chin-Kun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-8011ed5b2fc07576248238a640db7a9a6eecd14ee02e32506723f5b9a517f6383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) - chemistry</topic><topic>Animals</topic><topic>Circular Dichroism</topic><topic>Enzymes</topic><topic>Escherichia coli - metabolism</topic><topic>Hot Temperature</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Models, Statistical</topic><topic>Molecular biology</topic><topic>Molecular structure</topic><topic>Plasmids - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Temperature</topic><topic>Thermodynamics</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kouza, Maksim</creatorcontrib><creatorcontrib>Chang, Chi-Fon</creatorcontrib><creatorcontrib>Hayryan, Shura</creatorcontrib><creatorcontrib>Yu, Tsan-hung</creatorcontrib><creatorcontrib>Li, Mai Suan</creatorcontrib><creatorcontrib>Huang, Tai-huang</creatorcontrib><creatorcontrib>Hu, Chin-Kun</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kouza, Maksim</au><au>Chang, Chi-Fon</au><au>Hayryan, Shura</au><au>Yu, Tsan-hung</au><au>Li, Mai Suan</au><au>Huang, Tai-huang</au><au>Hu, Chin-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Folding of the Protein Domain hbSBD</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2005-11-01</date><risdate>2005</risdate><volume>89</volume><issue>5</issue><spage>3353</spage><epage>3361</epage><pages>3353-3361</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, which is well described by the two-state model with the folding temperature TF=317.8±1.95K and the enthalpy change ΔHG=19.67±2.67kcal/mol. The folding is also studied numerically using the off-lattice coarse-grained Go model and the Langevin dynamics. The obtained results, including the population of the native basin, the free-energy landscape as a function of the number of native contacts, and the folding kinetics, also suggest that the hbSBD domain is a two-state folder. These results are consistent with the biological function of hbSBD in branched-chain α-ketoacid dehydrogenase.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16126825</pmid><doi>10.1529/biophysj.105.065151</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 2005-11, Vol.89 (5), p.3353-3361 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1366832 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) - chemistry Animals Circular Dichroism Enzymes Escherichia coli - metabolism Hot Temperature Kinetics Models, Molecular Models, Statistical Molecular biology Molecular structure Plasmids - metabolism Protein Conformation Protein Denaturation Protein Folding Protein Structure, Tertiary Proteins Temperature Thermodynamics Time Factors |
| title | Folding of the Protein Domain hbSBD |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T21%3A12%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Folding%20of%20the%20Protein%20Domain%20hbSBD&rft.jtitle=Biophysical%20journal&rft.au=Kouza,%20Maksim&rft.date=2005-11-01&rft.volume=89&rft.issue=5&rft.spage=3353&rft.epage=3361&rft.pages=3353-3361&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1529/biophysj.105.065151&rft_dat=%3Cproquest_pubme%3E68735910%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=215700041&rft_id=info:pmid/16126825&rft_els_id=S0006349505729787&rfr_iscdi=true |