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Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride
Changes in the fluorescence spectrum of tryptophans Trp 134 and Trp 212 in bovine serum albumin (BSA) and of Trp 214 of human serum albumin in the presence of the chaotropic agent guanidine hydrochloride (Gnd) were studied. A detailed analysis of the fluorescence spectrum of native BSA yielded the f...
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| Published in: | Journal of Protein Chemistry 2000-08, Vol.19 (6), p.431-439 |
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| Main Authors: | , , , , |
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| cites | cdi_FETCH-LOGICAL-c456t-cb28f97fe1ccc8aa50aa858221ef6a83f56178eb5844a28041f01dfbc7ede1393 |
| container_end_page | 439 |
| container_issue | 6 |
| container_start_page | 431 |
| container_title | Journal of Protein Chemistry |
| container_volume | 19 |
| creator | Viallet, P M Vo-Dinh, T Ribou, A C Vigo, J Salmon, J M |
| description | Changes in the fluorescence spectrum of tryptophans Trp 134 and Trp 212 in bovine serum albumin (BSA) and of Trp 214 of human serum albumin in the presence of the chaotropic agent guanidine hydrochloride (Gnd) were studied. A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. Changes occurring when the Gnd concentration is decreased stepwise cover a larger concentration scale of Gnd than the reverse protocol, allowing one to suggest that the resulting conformational changes in the subdomain IA of BSA involve at least three different steps. |
| doi_str_mv | 10.1023/a:1026589012724 |
| format | article |
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A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. 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A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. Changes occurring when the Gnd concentration is decreased stepwise cover a larger concentration scale of Gnd than the reverse protocol, allowing one to suggest that the resulting conformational changes in the subdomain IA of BSA involve at least three different steps.</description><subject>Animals</subject><subject>Biophysics</subject><subject>Bovine serum albumin</subject><subject>Calcium - chemistry</subject><subject>Cattle</subject><subject>Energy transfer</subject><subject>Fluorescence</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Guanidine - pharmacology</subject><subject>Guanidine hydrochloride</subject><subject>Human serum albumin</subject><subject>Humans</subject><subject>Indo-1</subject><subject>Indoles - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Protein Binding - drug effects</subject><subject>Protein Conformation - drug effects</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Serum albumin</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>Tryptophan</subject><subject>Tryptophan - metabolism</subject><issn>0277-8033</issn><issn>1572-3887</issn><issn>1573-4943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNpdkU1v1DAQhi0EokvhzA1ZHHoL9UccO9yqqqWVKrjAOXLs8a6rxF7suFL_HL-tznYRoqfxxzPvvDOD0EdKvlDC-Ln-WkMnVE8ok6x9hTZUSN60fctfow1hUjaKcH6C3uV8TwjplSJv0QmltBd9Jzfoz3e9-AfAbioxQTYQDGAdLJ71tvHBxoY2-xQX8AH7sEDSZvExYJ3xEuOUsYsJV2D0YYtLcHGy62lVSPD3luF3WYUzjg4vO8BjfPAB6nsqM9bTWOYqn8to46wPhQ7Uvho6-KlZ26KDt2vS7tGmaHZTTN7Ce_TG6SnDh2M8Rb-ur35e3jR3P77dXl7cNaYV3dKYkSnXSwfUGKO0FkRrJRRjFFynFXeio1LBKFTbaqZISx2h1o1GggXKe36Kzp51a6u1l7wMs6_DmiYdIJY8SCYYJ31Xwc8vwPtYUqjehvoruGRMVuj8GTIp5lznNOyTn3V6HCgZ1r0OF8N_e60Zn46yZZzB_uOPi-RPYd6idg</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Viallet, P M</creator><creator>Vo-Dinh, T</creator><creator>Ribou, A C</creator><creator>Vigo, J</creator><creator>Salmon, J M</creator><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</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>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000801</creationdate><title>Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride</title><author>Viallet, P M ; Vo-Dinh, T ; Ribou, A C ; Vigo, J ; Salmon, J M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-cb28f97fe1ccc8aa50aa858221ef6a83f56178eb5844a28041f01dfbc7ede1393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Biophysics</topic><topic>Bovine serum albumin</topic><topic>Calcium - chemistry</topic><topic>Cattle</topic><topic>Energy transfer</topic><topic>Fluorescence</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Guanidine - pharmacology</topic><topic>Guanidine hydrochloride</topic><topic>Human serum albumin</topic><topic>Humans</topic><topic>Indo-1</topic><topic>Indoles - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular biology</topic><topic>Protein Binding - drug effects</topic><topic>Protein Conformation - drug effects</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Serum albumin</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>Tryptophan</topic><topic>Tryptophan - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Viallet, P M</creatorcontrib><creatorcontrib>Vo-Dinh, T</creatorcontrib><creatorcontrib>Ribou, A C</creatorcontrib><creatorcontrib>Vigo, J</creatorcontrib><creatorcontrib>Salmon, J M</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>ProQuest 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>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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</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>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>https://resources.nclive.org/materials</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</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 Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of Protein Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Viallet, P M</au><au>Vo-Dinh, T</au><au>Ribou, A C</au><au>Vigo, J</au><au>Salmon, J M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride</atitle><jtitle>Journal of Protein Chemistry</jtitle><addtitle>J Protein Chem</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>19</volume><issue>6</issue><spage>431</spage><epage>439</epage><pages>431-439</pages><issn>0277-8033</issn><issn>1572-3887</issn><eissn>1573-4943</eissn><abstract>Changes in the fluorescence spectrum of tryptophans Trp 134 and Trp 212 in bovine serum albumin (BSA) and of Trp 214 of human serum albumin in the presence of the chaotropic agent guanidine hydrochloride (Gnd) were studied. A detailed analysis of the fluorescence spectrum of native BSA yielded the fluorescence spectrum for each tryptophan of BSA. Modifications in the binding of Mag-indo-1 to BSA, which results in a specific quenching of the fluorescence spectrum of Trp 134 associated with an energy transfer from Trp 134 to the protein-bound Mag-indo-1, were also investigated. Changes occurring when the Gnd concentration is decreased stepwise cover a larger concentration scale of Gnd than the reverse protocol, allowing one to suggest that the resulting conformational changes in the subdomain IA of BSA involve at least three different steps.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>11195967</pmid><doi>10.1023/a:1026589012724</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0277-8033 |
| ispartof | Journal of Protein Chemistry, 2000-08, Vol.19 (6), p.431-439 |
| issn | 0277-8033 1572-3887 1573-4943 |
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| subjects | Animals Biophysics Bovine serum albumin Calcium - chemistry Cattle Energy transfer Fluorescence Fluorescent Dyes - chemistry Guanidine - pharmacology Guanidine hydrochloride Human serum albumin Humans Indo-1 Indoles - chemistry Models, Molecular Molecular biology Protein Binding - drug effects Protein Conformation - drug effects Protein Denaturation Protein Folding Proteins Serum albumin Serum Albumin, Bovine - chemistry Spectrometry, Fluorescence Tryptophan Tryptophan - metabolism |
| title | Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride |
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