Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR
Stereospecific assignments of the aspartic acid and asparagine, β-protons of the 108 residue protein E. coli thioredoxin have been obtained by the use of chiral deuteration. In addition protein samples have been prepared in which all carbon bound hydrogen positions are substituted to an extent of 75...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1987-10, Vol.223 (1), p.191-196 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 196 |
|---|---|
| container_issue | 1 |
| container_start_page | 191 |
| container_title | FEBS letters |
| container_volume | 223 |
| creator | LeMaster, David M. |
| description | Stereospecific assignments of the aspartic acid and asparagine, β-protons of the 108 residue protein
E. coli thioredoxin have been obtained by the use of chiral deuteration. In addition protein samples have been prepared in which all carbon bound hydrogen positions are substituted to an extent of 75% with deuterium. These random fractionally deuterated samples significantly facilitate the measurement of coupling constants and intraresidue NOE intensities which combined with the stereospecific assignments have provided determination of the first sidechain dihedral angle ϰ
1, for all four asparagine residues and eight of the ten assigned aspartic acid residues. |
| doi_str_mv | 10.1016/0014-5793(87)80534-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_81069459</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579387805343</els_id><sourcerecordid>14827069</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3953-12ac39cf5f183c47eb0571a7c35e0a006017107458c15855c97aebbc4830949f3</originalsourceid><addsrcrecordid>eNqNkcGOFCEQhonRrOPqG2jCwZj10AoDNHAx0cmOmqyaGD0Turo6w6a7WaFHM6-1D-IzSW9P5qheoPjrqwL-IuQpZ6844_VrxrislLbiwuiXhikhK3GPrLjRohKyNvfJ6oQ8JI9yvmblbLg9I2dCcG6YXZHrzS4k39Pft9SPLU1liQPtkocpxLEkWtxPmPx8ol1MdNph0Yo0hHFRY0dvUpwwjDSHFmHnSwRxLPSwEM2Bfv709TF50Pk-45Pjfk6-by-_bT5UV1_ef9y8vapAWCUqvvYlgE513AiQGhumNPcahELmGasZ15xpqQxwZZQCqz02DUgjmJW2E-fkxdK3vOrHHvPkhpAB-96PGPfZGc5qK5X9J8ilWevCFlAuIKSYc8LO3aQw-HRwnLl5Fm422s1GO6Pd3SycKGXPjv33zYDtqehofsk_P-Z9Bt8X00cI-YTp2gij1wXbLtiv0OPhv65228t36zkx60bfqfN73iyNsLj_M2ByGQKOgG1ICJNrY_j7h_4At0W4wg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14827069</pqid></control><display><type>article</type><title>Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>LeMaster, David M.</creator><creatorcontrib>LeMaster, David M.</creatorcontrib><description>Stereospecific assignments of the aspartic acid and asparagine, β-protons of the 108 residue protein
E. coli thioredoxin have been obtained by the use of chiral deuteration. In addition protein samples have been prepared in which all carbon bound hydrogen positions are substituted to an extent of 75% with deuterium. These random fractionally deuterated samples significantly facilitate the measurement of coupling constants and intraresidue NOE intensities which combined with the stereospecific assignments have provided determination of the first sidechain dihedral angle ϰ
1, for all four asparagine residues and eight of the ten assigned aspartic acid residues.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(87)80534-3</identifier><identifier>PMID: 3311809</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Asparagine ; Aspartic Acid ; Bacterial Proteins ; Biological and medical sciences ; Chiral deuteration ; deuteration ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Magnetic Resonance Spectroscopy - methods ; Molecular biophysics ; N.M.R ; Protein Conformation ; Protein NMR ; Sidechain conformation ; Stereoisomerism ; Structure in molecular biology ; thioredoxin ; Thioredoxins ; Tridimensional structure</subject><ispartof>FEBS letters, 1987-10, Vol.223 (1), p.191-196</ispartof><rights>1987</rights><rights>FEBS Letters 223 (1987) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3953-12ac39cf5f183c47eb0571a7c35e0a006017107458c15855c97aebbc4830949f3</citedby><cites>FETCH-LOGICAL-c3953-12ac39cf5f183c47eb0571a7c35e0a006017107458c15855c97aebbc4830949f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579387805343$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7683872$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3311809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LeMaster, David M.</creatorcontrib><title>Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Stereospecific assignments of the aspartic acid and asparagine, β-protons of the 108 residue protein
E. coli thioredoxin have been obtained by the use of chiral deuteration. In addition protein samples have been prepared in which all carbon bound hydrogen positions are substituted to an extent of 75% with deuterium. These random fractionally deuterated samples significantly facilitate the measurement of coupling constants and intraresidue NOE intensities which combined with the stereospecific assignments have provided determination of the first sidechain dihedral angle ϰ
1, for all four asparagine residues and eight of the ten assigned aspartic acid residues.</description><subject>Asparagine</subject><subject>Aspartic Acid</subject><subject>Bacterial Proteins</subject><subject>Biological and medical sciences</subject><subject>Chiral deuteration</subject><subject>deuteration</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Molecular biophysics</subject><subject>N.M.R</subject><subject>Protein Conformation</subject><subject>Protein NMR</subject><subject>Sidechain conformation</subject><subject>Stereoisomerism</subject><subject>Structure in molecular biology</subject><subject>thioredoxin</subject><subject>Thioredoxins</subject><subject>Tridimensional structure</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcGOFCEQhonRrOPqG2jCwZj10AoDNHAx0cmOmqyaGD0Turo6w6a7WaFHM6-1D-IzSW9P5qheoPjrqwL-IuQpZ6844_VrxrislLbiwuiXhikhK3GPrLjRohKyNvfJ6oQ8JI9yvmblbLg9I2dCcG6YXZHrzS4k39Pft9SPLU1liQPtkocpxLEkWtxPmPx8ol1MdNph0Yo0hHFRY0dvUpwwjDSHFmHnSwRxLPSwEM2Bfv709TF50Pk-45Pjfk6-by-_bT5UV1_ef9y8vapAWCUqvvYlgE513AiQGhumNPcahELmGasZ15xpqQxwZZQCqz02DUgjmJW2E-fkxdK3vOrHHvPkhpAB-96PGPfZGc5qK5X9J8ilWevCFlAuIKSYc8LO3aQw-HRwnLl5Fm422s1GO6Pd3SycKGXPjv33zYDtqehofsk_P-Z9Bt8X00cI-YTp2gij1wXbLtiv0OPhv65228t36zkx60bfqfN73iyNsLj_M2ByGQKOgG1ICJNrY_j7h_4At0W4wg</recordid><startdate>19871019</startdate><enddate>19871019</enddate><creator>LeMaster, David M.</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>19871019</creationdate><title>Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR</title><author>LeMaster, David M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3953-12ac39cf5f183c47eb0571a7c35e0a006017107458c15855c97aebbc4830949f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Asparagine</topic><topic>Aspartic Acid</topic><topic>Bacterial Proteins</topic><topic>Biological and medical sciences</topic><topic>Chiral deuteration</topic><topic>deuteration</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Molecular biophysics</topic><topic>N.M.R</topic><topic>Protein Conformation</topic><topic>Protein NMR</topic><topic>Sidechain conformation</topic><topic>Stereoisomerism</topic><topic>Structure in molecular biology</topic><topic>thioredoxin</topic><topic>Thioredoxins</topic><topic>Tridimensional structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LeMaster, David M.</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>LeMaster, David M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1987-10-19</date><risdate>1987</risdate><volume>223</volume><issue>1</issue><spage>191</spage><epage>196</epage><pages>191-196</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Stereospecific assignments of the aspartic acid and asparagine, β-protons of the 108 residue protein
E. coli thioredoxin have been obtained by the use of chiral deuteration. In addition protein samples have been prepared in which all carbon bound hydrogen positions are substituted to an extent of 75% with deuterium. These random fractionally deuterated samples significantly facilitate the measurement of coupling constants and intraresidue NOE intensities which combined with the stereospecific assignments have provided determination of the first sidechain dihedral angle ϰ
1, for all four asparagine residues and eight of the ten assigned aspartic acid residues.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3311809</pmid><doi>10.1016/0014-5793(87)80534-3</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1987-10, Vol.223 (1), p.191-196 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81069459 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Asparagine Aspartic Acid Bacterial Proteins Biological and medical sciences Chiral deuteration deuteration Escherichia coli Fundamental and applied biological sciences. Psychology Magnetic Resonance Spectroscopy - methods Molecular biophysics N.M.R Protein Conformation Protein NMR Sidechain conformation Stereoisomerism Structure in molecular biology thioredoxin Thioredoxins Tridimensional structure |
| title | Chiral β and random fractional deuteration for the determination of protein sidechain conformation by NMR |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T20%3A40%3A04IST&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=Chiral%20%CE%B2%20and%20random%20fractional%20deuteration%20for%20the%20determination%20of%20protein%20sidechain%20conformation%20by%20NMR&rft.jtitle=FEBS%20letters&rft.au=LeMaster,%20David%20M.&rft.date=1987-10-19&rft.volume=223&rft.issue=1&rft.spage=191&rft.epage=196&rft.pages=191-196&rft.issn=0014-5793&rft.eissn=1873-3468&rft.coden=FEBLAL&rft_id=info:doi/10.1016/0014-5793(87)80534-3&rft_dat=%3Cproquest_cross%3E14827069%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=14827069&rft_id=info:pmid/3311809&rft_els_id=0014579387805343&rfr_iscdi=true |