Fluorescence quenching studies with proteins
A review is presented on the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins. A number of factors are discussed that must be considered in analyzing such data. Among these factors are the efficiency of the quenching process, the relative importan...
Gespeichert in:
| Veröffentlicht in: | Analytical Biochemistry 1981-07, Vol.114 (2), p.199-227 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 227 |
|---|---|
| container_issue | 2 |
| container_start_page | 199 |
| container_title | Analytical Biochemistry |
| container_volume | 114 |
| creator | Eftink, Maurice R. Ghiron, Camillo A. |
| description | A review is presented on the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins. A number of factors are discussed that must be considered in analyzing such data. Among these factors are the efficiency of the quenching process, the relative importance of static quenching, the heterogeneity of the emission, and the tendency of the quencher to interact with the protein. |
| doi_str_mv | 10.1016/0003-2697(81)90474-7 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73732873</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0003269781904747</els_id><sourcerecordid>15349223</sourcerecordid><originalsourceid>FETCH-LOGICAL-c419t-b960f9b14937d1724ed69aaf0aa98bad68a28ae320d42d1324573d198d5740493</originalsourceid><addsrcrecordid>eNqNkMFKxDAQhoMo67r6Bgp7EgWrM0naNBdBFleFBS96DmmTupFuq0mr-Pam7rJH9TSH-eafn4-QY4RLBMyuAIAlNJPiLMdzCVzwROyQMYLMEmAgd8l4i-yTgxBeARB5mo3ISEQAKR2Ti3ndt96G0jalnb73cSxd8zINXW-cDdNP1y2nb77trGvCIdmrdB3s0WZOyPP89ml2nywe7x5mN4uk5Ci7pJAZVLJALpkwKCi3JpNaV6C1zAttslzTXFtGwXBqkFGeCmZQ5iYVHOLVhJyuc-PjWCl0auViw7rWjW37oAQTjOaC_Qliyjlilv4DZFxSOiTyNVj6NgRvK_Xm3Ur7L4WgBu1qcKoGpypH9aM99pmQk01-X6ys2R5tPMf99Xpvo7YPZ70KpRuUG-dt2SnTut8ffAOKeo8z</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15349223</pqid></control><display><type>article</type><title>Fluorescence quenching studies with proteins</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Eftink, Maurice R. ; Ghiron, Camillo A.</creator><creatorcontrib>Eftink, Maurice R. ; Ghiron, Camillo A.</creatorcontrib><description>A review is presented on the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins. A number of factors are discussed that must be considered in analyzing such data. Among these factors are the efficiency of the quenching process, the relative importance of static quenching, the heterogeneity of the emission, and the tendency of the quencher to interact with the protein.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(81)90474-7</identifier><identifier>PMID: 7030122</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetamides ; Acrylamide ; Acrylamides ; Alcohol Oxidoreductases ; Azurin ; Chemical Phenomena ; Chemistry, Physical ; dynamics ; Ethylene Chlorohydrin - analogs & derivatives ; Fluorescence ; Hydrogen Peroxide ; Indoles ; Kinetics ; Liver - enzymology ; Luminescent Measurements ; Mathematics ; Plant Proteins ; Proteins ; Pyridinium Compounds ; reviews ; Sodium Iodide ; structure ; Succinimides ; Tryptophan ; Tyrosine</subject><ispartof>Analytical Biochemistry, 1981-07, Vol.114 (2), p.199-227</ispartof><rights>1981</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-b960f9b14937d1724ed69aaf0aa98bad68a28ae320d42d1324573d198d5740493</citedby><cites>FETCH-LOGICAL-c419t-b960f9b14937d1724ed69aaf0aa98bad68a28ae320d42d1324573d198d5740493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-2697(81)90474-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>313,314,780,784,792,3550,27922,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7030122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Eftink, Maurice R.</creatorcontrib><creatorcontrib>Ghiron, Camillo A.</creatorcontrib><title>Fluorescence quenching studies with proteins</title><title>Analytical Biochemistry</title><addtitle>Anal Biochem</addtitle><description>A review is presented on the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins. A number of factors are discussed that must be considered in analyzing such data. Among these factors are the efficiency of the quenching process, the relative importance of static quenching, the heterogeneity of the emission, and the tendency of the quencher to interact with the protein.</description><subject>Acetamides</subject><subject>Acrylamide</subject><subject>Acrylamides</subject><subject>Alcohol Oxidoreductases</subject><subject>Azurin</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>dynamics</subject><subject>Ethylene Chlorohydrin - analogs & derivatives</subject><subject>Fluorescence</subject><subject>Hydrogen Peroxide</subject><subject>Indoles</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Luminescent Measurements</subject><subject>Mathematics</subject><subject>Plant Proteins</subject><subject>Proteins</subject><subject>Pyridinium Compounds</subject><subject>reviews</subject><subject>Sodium Iodide</subject><subject>structure</subject><subject>Succinimides</subject><subject>Tryptophan</subject><subject>Tyrosine</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMFKxDAQhoMo67r6Bgp7EgWrM0naNBdBFleFBS96DmmTupFuq0mr-Pam7rJH9TSH-eafn4-QY4RLBMyuAIAlNJPiLMdzCVzwROyQMYLMEmAgd8l4i-yTgxBeARB5mo3ISEQAKR2Ti3ndt96G0jalnb73cSxd8zINXW-cDdNP1y2nb77trGvCIdmrdB3s0WZOyPP89ml2nywe7x5mN4uk5Ci7pJAZVLJALpkwKCi3JpNaV6C1zAttslzTXFtGwXBqkFGeCmZQ5iYVHOLVhJyuc-PjWCl0auViw7rWjW37oAQTjOaC_Qliyjlilv4DZFxSOiTyNVj6NgRvK_Xm3Ur7L4WgBu1qcKoGpypH9aM99pmQk01-X6ys2R5tPMf99Xpvo7YPZ70KpRuUG-dt2SnTut8ffAOKeo8z</recordid><startdate>19810701</startdate><enddate>19810701</enddate><creator>Eftink, Maurice R.</creator><creator>Ghiron, Camillo A.</creator><general>Elsevier 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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19810701</creationdate><title>Fluorescence quenching studies with proteins</title><author>Eftink, Maurice R. ; Ghiron, Camillo A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-b960f9b14937d1724ed69aaf0aa98bad68a28ae320d42d1324573d198d5740493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Acetamides</topic><topic>Acrylamide</topic><topic>Acrylamides</topic><topic>Alcohol Oxidoreductases</topic><topic>Azurin</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>dynamics</topic><topic>Ethylene Chlorohydrin - analogs & derivatives</topic><topic>Fluorescence</topic><topic>Hydrogen Peroxide</topic><topic>Indoles</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Luminescent Measurements</topic><topic>Mathematics</topic><topic>Plant Proteins</topic><topic>Proteins</topic><topic>Pyridinium Compounds</topic><topic>reviews</topic><topic>Sodium Iodide</topic><topic>structure</topic><topic>Succinimides</topic><topic>Tryptophan</topic><topic>Tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eftink, Maurice R.</creatorcontrib><creatorcontrib>Ghiron, Camillo A.</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>Analytical Biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eftink, Maurice R.</au><au>Ghiron, Camillo A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fluorescence quenching studies with proteins</atitle><jtitle>Analytical Biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1981-07-01</date><risdate>1981</risdate><volume>114</volume><issue>2</issue><spage>199</spage><epage>227</epage><pages>199-227</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>A review is presented on the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins. A number of factors are discussed that must be considered in analyzing such data. Among these factors are the efficiency of the quenching process, the relative importance of static quenching, the heterogeneity of the emission, and the tendency of the quencher to interact with the protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7030122</pmid><doi>10.1016/0003-2697(81)90474-7</doi><tpages>29</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2697 |
| ispartof | Analytical Biochemistry, 1981-07, Vol.114 (2), p.199-227 |
| issn | 0003-2697 1096-0309 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73732873 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Acetamides Acrylamide Acrylamides Alcohol Oxidoreductases Azurin Chemical Phenomena Chemistry, Physical dynamics Ethylene Chlorohydrin - analogs & derivatives Fluorescence Hydrogen Peroxide Indoles Kinetics Liver - enzymology Luminescent Measurements Mathematics Plant Proteins Proteins Pyridinium Compounds reviews Sodium Iodide structure Succinimides Tryptophan Tyrosine |
| title | Fluorescence quenching studies with proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T02%3A52%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Fluorescence%20quenching%20studies%20with%20proteins&rft.jtitle=Analytical%20Biochemistry&rft.au=Eftink,%20Maurice%20R.&rft.date=1981-07-01&rft.volume=114&rft.issue=2&rft.spage=199&rft.epage=227&rft.pages=199-227&rft.issn=0003-2697&rft.eissn=1096-0309&rft_id=info:doi/10.1016/0003-2697(81)90474-7&rft_dat=%3Cproquest_cross%3E15349223%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15349223&rft_id=info:pmid/7030122&rft_els_id=0003269781904747&rfr_iscdi=true |