An Approach to NMR Assignment of Intrinsically Disordered Proteins
An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in [15N,13C′]‐ and [13C′,1HN]‐correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D (HACA)CON(CA)HA} spectra...
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| Veröffentlicht in: | Chemphyschem 2015-03, Vol.16 (4), p.739-746 |
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| creator | Goradia, Nishit Wiedemann, Christoph Herbst, Christian Görlach, Matthias Heinemann, Stefan H. Ohlenschläger, Oliver Ramachandran, Ramadurai |
| description | An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in [15N,13C′]‐ and [13C′,1HN]‐correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D (HACA)CON(CA)HA} spectra for backbone assignments via sequential HN and Hα correlations and {3D (H)NCO(CACS)HS and 3D (HS)CS(CA)CO(N)H} spectra for side‐chain 1H and 13C assignments, employing sequential 1H data acquisitions with direct detection of both the amide and aliphatic protons. The efficacy of the approach for obtaining resonance assignments with complete backbone and side‐chain chemical shifts is demonstrated experimentally for the 61‐residue [13C,15N]‐labelled peptide of a voltage‐gated potassium channel protein of the Kv1.4 channel subunit. The general applicability of the approach for the characterisation of moderately sized globular proteins is also demonstrated.
Order, please! A robust and efficient approach to the NMR assignment of intrinsically disordered proteins and protein regions involving sequential data acquisitions with direct detection of both the amide and aliphatic protons is presented. |
| doi_str_mv | 10.1002/cphc.201402872 |
| format | Article |
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Order, please! A robust and efficient approach to the NMR assignment of intrinsically disordered proteins and protein regions involving sequential data acquisitions with direct detection of both the amide and aliphatic protons is presented.</description><identifier>ISSN: 1439-4235</identifier><identifier>EISSN: 1439-7641</identifier><identifier>DOI: 10.1002/cphc.201402872</identifier><identifier>PMID: 25639453</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>haem regulatory motifs ; intrinsically disordered proteins ; Intrinsically Disordered Proteins - chemistry ; ion channels ; Magnetic Resonance Spectroscopy - methods ; Magnetic Resonance Spectroscopy - standards ; nmr spectroscopy ; Potassium ; Proteins ; Reference Standards ; sequential data acquisition</subject><ispartof>Chemphyschem, 2015-03, Vol.16 (4), p.739-746</ispartof><rights>2015 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5582-ca2e1cbd847129eb58692371ff1b15eaadf525036fe2fc13eea5bbd7f2a9e84b3</citedby><cites>FETCH-LOGICAL-c5582-ca2e1cbd847129eb58692371ff1b15eaadf525036fe2fc13eea5bbd7f2a9e84b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcphc.201402872$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcphc.201402872$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25639453$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goradia, Nishit</creatorcontrib><creatorcontrib>Wiedemann, Christoph</creatorcontrib><creatorcontrib>Herbst, Christian</creatorcontrib><creatorcontrib>Görlach, Matthias</creatorcontrib><creatorcontrib>Heinemann, Stefan H.</creatorcontrib><creatorcontrib>Ohlenschläger, Oliver</creatorcontrib><creatorcontrib>Ramachandran, Ramadurai</creatorcontrib><title>An Approach to NMR Assignment of Intrinsically Disordered Proteins</title><title>Chemphyschem</title><addtitle>ChemPhysChem</addtitle><description>An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in [15N,13C′]‐ and [13C′,1HN]‐correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D (HACA)CON(CA)HA} spectra for backbone assignments via sequential HN and Hα correlations and {3D (H)NCO(CACS)HS and 3D (HS)CS(CA)CO(N)H} spectra for side‐chain 1H and 13C assignments, employing sequential 1H data acquisitions with direct detection of both the amide and aliphatic protons. The efficacy of the approach for obtaining resonance assignments with complete backbone and side‐chain chemical shifts is demonstrated experimentally for the 61‐residue [13C,15N]‐labelled peptide of a voltage‐gated potassium channel protein of the Kv1.4 channel subunit. The general applicability of the approach for the characterisation of moderately sized globular proteins is also demonstrated.
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A robust and efficient approach to the NMR assignment of intrinsically disordered proteins and protein regions involving sequential data acquisitions with direct detection of both the amide and aliphatic protons is presented.</description><subject>haem regulatory motifs</subject><subject>intrinsically disordered proteins</subject><subject>Intrinsically Disordered Proteins - chemistry</subject><subject>ion channels</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Magnetic Resonance Spectroscopy - standards</subject><subject>nmr spectroscopy</subject><subject>Potassium</subject><subject>Proteins</subject><subject>Reference Standards</subject><subject>sequential data acquisition</subject><issn>1439-4235</issn><issn>1439-7641</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkElPwzAQhS0EYilcOaJIXLik2GM7y7GErWIVAoG4WI4zhkCaFDsV9N-TqqVCXDjNSPO9pzePkF1G-4xSODTjV9MHygSFJIYVsskET8M4Emx1sQvgcoNsef9GKU1ozNbJBsiIp0LyTXI0qIPBeOwabV6Dtgmur-6CgfflSz3Cug0aGwzr1pW1L42uqmlwXPrGFeiwCG5d02J32SZrVlcedxazRx5OT-6z8_Dy5myYDS5DI2UCodGAzORFImIGKeYyiVLgMbOW5Uyi1oWVICmPLII1jCNqmedFbEGnmIic98jB3LdL-zFB36pR6Q1Wla6xmXjFoggi0f0oO3T_D_rWTFzdpZtRLJWQguio_pwyrvHeoVVjV460mypG1axdNWtXLdvtBHsL20k-wmKJ_9TZAekc-CwrnP5jp7Lb8-y3eTjXlr7Fr6VWu3cVxTyW6vH6TDG4eD59Os7UI_8GaR2UsQ</recordid><startdate>20150316</startdate><enddate>20150316</enddate><creator>Goradia, Nishit</creator><creator>Wiedemann, Christoph</creator><creator>Herbst, Christian</creator><creator>Görlach, Matthias</creator><creator>Heinemann, Stefan H.</creator><creator>Ohlenschläger, Oliver</creator><creator>Ramachandran, Ramadurai</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>K9.</scope><scope>7X8</scope></search><sort><creationdate>20150316</creationdate><title>An Approach to NMR Assignment of Intrinsically Disordered Proteins</title><author>Goradia, Nishit ; Wiedemann, Christoph ; Herbst, Christian ; Görlach, Matthias ; Heinemann, Stefan H. ; Ohlenschläger, Oliver ; Ramachandran, Ramadurai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5582-ca2e1cbd847129eb58692371ff1b15eaadf525036fe2fc13eea5bbd7f2a9e84b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>haem regulatory motifs</topic><topic>intrinsically disordered proteins</topic><topic>Intrinsically Disordered Proteins - chemistry</topic><topic>ion channels</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Magnetic Resonance Spectroscopy - standards</topic><topic>nmr spectroscopy</topic><topic>Potassium</topic><topic>Proteins</topic><topic>Reference Standards</topic><topic>sequential data acquisition</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goradia, Nishit</creatorcontrib><creatorcontrib>Wiedemann, Christoph</creatorcontrib><creatorcontrib>Herbst, Christian</creatorcontrib><creatorcontrib>Görlach, Matthias</creatorcontrib><creatorcontrib>Heinemann, Stefan H.</creatorcontrib><creatorcontrib>Ohlenschläger, Oliver</creatorcontrib><creatorcontrib>Ramachandran, Ramadurai</creatorcontrib><collection>Istex</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 Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Chemphyschem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goradia, Nishit</au><au>Wiedemann, Christoph</au><au>Herbst, Christian</au><au>Görlach, Matthias</au><au>Heinemann, Stefan H.</au><au>Ohlenschläger, Oliver</au><au>Ramachandran, Ramadurai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An Approach to NMR Assignment of Intrinsically Disordered Proteins</atitle><jtitle>Chemphyschem</jtitle><addtitle>ChemPhysChem</addtitle><date>2015-03-16</date><risdate>2015</risdate><volume>16</volume><issue>4</issue><spage>739</spage><epage>746</epage><pages>739-746</pages><issn>1439-4235</issn><eissn>1439-7641</eissn><abstract>An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in [15N,13C′]‐ and [13C′,1HN]‐correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D (HACA)CON(CA)HA} spectra for backbone assignments via sequential HN and Hα correlations and {3D (H)NCO(CACS)HS and 3D (HS)CS(CA)CO(N)H} spectra for side‐chain 1H and 13C assignments, employing sequential 1H data acquisitions with direct detection of both the amide and aliphatic protons. The efficacy of the approach for obtaining resonance assignments with complete backbone and side‐chain chemical shifts is demonstrated experimentally for the 61‐residue [13C,15N]‐labelled peptide of a voltage‐gated potassium channel protein of the Kv1.4 channel subunit. The general applicability of the approach for the characterisation of moderately sized globular proteins is also demonstrated.
Order, please! A robust and efficient approach to the NMR assignment of intrinsically disordered proteins and protein regions involving sequential data acquisitions with direct detection of both the amide and aliphatic protons is presented.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>25639453</pmid><doi>10.1002/cphc.201402872</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | haem regulatory motifs intrinsically disordered proteins Intrinsically Disordered Proteins - chemistry ion channels Magnetic Resonance Spectroscopy - methods Magnetic Resonance Spectroscopy - standards nmr spectroscopy Potassium Proteins Reference Standards sequential data acquisition |
| title | An Approach to NMR Assignment of Intrinsically Disordered Proteins |
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