000140004 001__ 140004
000140004 005__ 20210129212739.0
000140004 0247_ $$2doi$$a10.1021/bi401020t
000140004 0247_ $$2ISSN$$a1520-4995
000140004 0247_ $$2ISSN$$a0006-2960
000140004 0247_ $$2WOS$$aWOS:000326355500011
000140004 0247_ $$2altmetric$$aaltmetric:1785604
000140004 0247_ $$2pmid$$apmid:24033104
000140004 037__ $$aFZJ-2013-05971
000140004 041__ $$aEnglish
000140004 082__ $$a570
000140004 1001_ $$0P:(DE-Juel1)132026$$aVarghese, Sabu$$b0$$ufzj
000140004 245__ $$aExpression, Purification, and Solid-State NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in Two Electronic Spin States
000140004 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2013
000140004 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1385708350_8169
000140004 3367_ $$2DataCite$$aOutput Types/Journal article
000140004 3367_ $$00$$2EndNote$$aJournal Article
000140004 3367_ $$2BibTeX$$aARTICLE
000140004 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000140004 3367_ $$2DRIVER$$aarticle
000140004 500__ $$3POF3_Assignment on 2016-02-29
000140004 520__ $$aThe nitrophorins (NPs) comprise a group of NO transporting ferriheme b proteins found in the saliva of the blood sucking insect Rhodnius prolixus. In contrast to other nitrophorins (NP1–4), the recently identified membrane binding isoform NP7 tends to form oligomers and precipitates at higher concentrations in solution. Hence, solid-state NMR (ssNMR) was employed as an alternative method to gain structural insights on the precipitated protein. We report the expression and purification of 13C,15N isotopically labeled protein together with the first ssNMR characterization of NP7. Because the size of NP7 (21 kDa) still provides a challenge for ssNMR, the samples were reverse labeled with Lys and Val to reduce the number of crosspeaks in two-dimensional spectra. The two electronic spin states with S = 1/2 and S = 0 at the ferriheme iron were generated by the complexation with imidazole and NO, respectively. ssNMR spectra of both forms are well resolved, which allows for sequential resonance assignments of 22 residues. Importantly, the ssNMR spectra demonstrate that aggregation does not affect the protein fold. Comparison of the spectra of the two electronic spin states allows the determination of paramagnetically shifted cross peaks due to pseudocontact shifts, which assists the assignment of residues close to the heme center.
000140004 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000140004 588__ $$aDataset connected to CrossRef, juser.fz-juelich.de
000140004 7001_ $$0P:(DE-HGF)0$$aYang, Fei$$b1
000140004 7001_ $$0P:(DE-HGF)0$$aPacheco, Victor$$b2
000140004 7001_ $$0P:(DE-HGF)0$$aWrede, Kathrin$$b3
000140004 7001_ $$0P:(DE-Juel1)156409$$aMedvedev, Alexander$$b4$$ufzj
000140004 7001_ $$0P:(DE-HGF)0$$aOgata, Hideaki$$b5
000140004 7001_ $$0P:(DE-HGF)0$$aKnipp, Markus$$b6$$eCorresponding author
000140004 7001_ $$0P:(DE-Juel1)132002$$aHeise, Henrike$$b7$$ufzj
000140004 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi401020t$$gVol. 52, no. 40, p. 7031 - 7040$$n40$$p7031 - 7040$$tBiochemistry$$v52$$x1520-4995$$y2013
000140004 8564_ $$uhttp://pubs.acs.org/doi/abs/10.1021/bi401020t
000140004 8564_ $$uhttps://juser.fz-juelich.de/record/140004/files/FZJ-2013-05971.pdf$$yRestricted
000140004 909CO $$ooai:juser.fz-juelich.de:140004$$pVDB
000140004 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132026$$aForschungszentrum Jülich GmbH$$b0$$kFZJ
000140004 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)156409$$aForschungszentrum Jülich GmbH$$b4$$kFZJ
000140004 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132002$$aForschungszentrum Jülich GmbH$$b7$$kFZJ
000140004 9132_ $$0G:(DE-HGF)POF3-559H$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vAddenda$$x0
000140004 9131_ $$0G:(DE-HGF)POF2-452$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$aDE-HGF$$bSchlüsseltechnologien$$lBioSoft$$vStructural Biology$$x0
000140004 9141_ $$y2013
000140004 915__ $$0StatID:(DE-HGF)0010$$2StatID$$aJCR/ISI refereed
000140004 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000140004 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000140004 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000140004 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000140004 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000140004 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000140004 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000140004 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000140004 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000140004 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000140004 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000140004 920__ $$lyes
000140004 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000140004 980__ $$ajournal
000140004 980__ $$aVDB
000140004 980__ $$aUNRESTRICTED
000140004 980__ $$aI:(DE-Juel1)ICS-6-20110106
000140004 981__ $$aI:(DE-Juel1)IBI-7-20200312