The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan
Studies of the absorption and fluorescence properties of the chaperone protein groEL (cpn60) from Escherichia coli show that tryptophan is present, in contrast to the proposed amino acid sequence of the protein (Hemmingsen, S.M. et al. (1988) Nature 333, 330–334). By determining a suitable value for...
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| Veröffentlicht in: | FEBS letters 1991-11, Vol.292 (1), p.9-12 |
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| creator | Price, Nicholas C. Kelly, Sharon M. Wood, Stephen auf der Mauer, Arlene |
| description | Studies of the absorption and fluorescence properties of the chaperone protein groEL (cpn60) from
Escherichia coli show that tryptophan is present, in contrast to the proposed amino acid sequence of the protein (Hemmingsen, S.M. et al. (1988) Nature 333, 330–334). By determining a suitable value for the specific absorption coefficient of the protein at 280 nm, it has been shown that the content of the aromatic amino acids corresponds to a single tryptophan and (most probably) seven tyrosines per subunit (
M
r 57 200). |
| doi_str_mv | 10.1016/0014-5793(91)80821-J |
| format | Article |
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Escherichia coli show that tryptophan is present, in contrast to the proposed amino acid sequence of the protein (Hemmingsen, S.M. et al. (1988) Nature 333, 330–334). By determining a suitable value for the specific absorption coefficient of the protein at 280 nm, it has been shown that the content of the aromatic amino acids corresponds to a single tryptophan and (most probably) seven tyrosines per subunit (
M
r 57 200).</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(91)80821-J</identifier><identifier>PMID: 1683633</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acids - analysis ; Analytical, structural and metabolic biochemistry ; Bacterial Proteins - chemistry ; Biological and medical sciences ; Chaperone protein ; Chaperonin 60 ; Chromatography, Gel ; Chromatography, Ion Exchange ; circular dichroism ; e d ; Escherichia coli ; Escherichia coli - metabolism ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; GdnHCl ; guanidinium chloride ; Heat-Shock Proteins - chemistry ; Miscellaneous ; Proteins ; Spectrometry, Fluorescence ; Spectrophotometry ; Tryptophan - analysis</subject><ispartof>FEBS letters, 1991-11, Vol.292 (1), p.9-12</ispartof><rights>1991 Federation of European Biochemical Societies</rights><rights>FEBS Letters 292 (1991) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526J-15f312199df8d3e0067d5bd67187f69ec2c0feaf525f44c582990b686cdc1e923</citedby><cites>FETCH-LOGICAL-c526J-15f312199df8d3e0067d5bd67187f69ec2c0feaf525f44c582990b686cdc1e923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(91)80821-J$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5008840$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1683633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Price, Nicholas C.</creatorcontrib><creatorcontrib>Kelly, Sharon M.</creatorcontrib><creatorcontrib>Wood, Stephen</creatorcontrib><creatorcontrib>auf der Mauer, Arlene</creatorcontrib><title>The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Studies of the absorption and fluorescence properties of the chaperone protein groEL (cpn60) from
Escherichia coli show that tryptophan is present, in contrast to the proposed amino acid sequence of the protein (Hemmingsen, S.M. et al. (1988) Nature 333, 330–334). By determining a suitable value for the specific absorption coefficient of the protein at 280 nm, it has been shown that the content of the aromatic amino acids corresponds to a single tryptophan and (most probably) seven tyrosines per subunit (
M
r 57 200).</description><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Chaperone protein</subject><subject>Chaperonin 60</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>circular dichroism</subject><subject>e d</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GdnHCl</subject><subject>guanidinium chloride</subject><subject>Heat-Shock Proteins - chemistry</subject><subject>Miscellaneous</subject><subject>Proteins</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry</subject><subject>Tryptophan - analysis</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU2P0zAQhiMEWsrCPwDJB4R2DwF_JI59QYJVC1SVuCxny3XGW6PUDra7qEf-OU5TLTfgZHnmmXc-3qp6SfBbggl_hzFp6raT7EqSa4EFJfX6UbUgomM1a7h4XC0ekKfVs5S-4_IXRF5UF4QLxhlbVL9ud4B0DHudnUF673xA2rgemeAz-IyCRbkgW20yRKcHZHZ6hBg8oDGGDM6juxiWG3RlRs_xNVreux68AWRDPJWOEdIpUKQ0Ss7fDYByPI45jDvtn1dPrB4SvDi_l9W31fL25nO9-frpy82HTW1aytc1aS0jlEjZW9EzwJh3fbvteVf2tVyCoQZb0LalrW0a0woqJd5ywU1vCEjKLqs3s24Z-8cBUlZ7lwwMg_YQDkl1tMW8Zd0_QcIbSSUTBWxm0MSQUgSrxuj2Oh4VwWqySE33V9P9lSTqZJFal7JXZ_3Ddg_9n6LZk5J_fc7rZPRgo_bGpQesxViIBhdsNWM_3QDH_2qtVsuPdEpMcUlO0Wme97MQlOvfO4gqGTcZ1rsIJqs-uL8v9Bse58BV</recordid><startdate>19911104</startdate><enddate>19911104</enddate><creator>Price, Nicholas C.</creator><creator>Kelly, Sharon M.</creator><creator>Wood, Stephen</creator><creator>auf der Mauer, Arlene</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19911104</creationdate><title>The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan</title><author>Price, Nicholas C. ; Kelly, Sharon M. ; Wood, Stephen ; auf der Mauer, Arlene</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526J-15f312199df8d3e0067d5bd67187f69ec2c0feaf525f44c582990b686cdc1e923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acids - analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biological and medical sciences</topic><topic>Chaperone protein</topic><topic>Chaperonin 60</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>circular dichroism</topic><topic>e d</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Fluorescence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GdnHCl</topic><topic>guanidinium chloride</topic><topic>Heat-Shock Proteins - chemistry</topic><topic>Miscellaneous</topic><topic>Proteins</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry</topic><topic>Tryptophan - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Price, Nicholas C.</creatorcontrib><creatorcontrib>Kelly, Sharon M.</creatorcontrib><creatorcontrib>Wood, Stephen</creatorcontrib><creatorcontrib>auf der Mauer, Arlene</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Price, Nicholas C.</au><au>Kelly, Sharon M.</au><au>Wood, Stephen</au><au>auf der Mauer, Arlene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1991-11-04</date><risdate>1991</risdate><volume>292</volume><issue>1</issue><spage>9</spage><epage>12</epage><pages>9-12</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Studies of the absorption and fluorescence properties of the chaperone protein groEL (cpn60) from
Escherichia coli show that tryptophan is present, in contrast to the proposed amino acid sequence of the protein (Hemmingsen, S.M. et al. (1988) Nature 333, 330–334). By determining a suitable value for the specific absorption coefficient of the protein at 280 nm, it has been shown that the content of the aromatic amino acids corresponds to a single tryptophan and (most probably) seven tyrosines per subunit (
M
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| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1991-11, Vol.292 (1), p.9-12 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Biological and medical sciences Chaperone protein Chaperonin 60 Chromatography, Gel Chromatography, Ion Exchange circular dichroism e d Escherichia coli Escherichia coli - metabolism Fluorescence Fundamental and applied biological sciences. Psychology GdnHCl guanidinium chloride Heat-Shock Proteins - chemistry Miscellaneous Proteins Spectrometry, Fluorescence Spectrophotometry Tryptophan - analysis |
| title | The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan |
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