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dc.contributor.authorKarjalainen, Mikael
dc.contributor.authorTossavainen, Helena
dc.contributor.authorHellman, Maarit
dc.contributor.authorPermi, Perttu
dc.date.accessioned2020-11-02T07:34:38Z
dc.date.available2020-11-02T07:34:38Z
dc.date.issued2020
dc.identifier.citationKarjalainen, M., Tossavainen, H., Hellman, M., & Permi, P. (2020). HACANCOi : a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins. <i>Journal of Biomolecular NMR</i>, <i>74</i>(12), 741-752. <a href="https://doi.org/10.1007/s10858-020-00347-5" target="_blank">https://doi.org/10.1007/s10858-020-00347-5</a>
dc.identifier.otherCONVID_43418478
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/72423
dc.description.abstractUnidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T2) relaxation times allowing sophisticated coherence transfer pathway selection in comparison to folded proteins. 1Hα-detection ensures non-susceptibility to chemical exchange with the solvent and enables chemical shift assignment of consecutive proline residues, typically abundant in IDPs. However, many IDPs undergo a disorder-to-order transition upon interaction with their target protein, which leads to the loss of the favorable relaxation properties. Long coherence transfer routes now result in prohibitively large decrease in sensitivity. We introduce a novel 4D 1Hα-detected experiment HACANCOi, together with its 3D implementation, which warrant high sensitivity for the assignment of proline-rich regions in IDPs in complex with a globular protein. The experiment correlates 1Hαi, 13Cαi, 15Ni and 13C′i13Ci′ spins by transferring the magnetization concomitantly from 13Cαi to 15Ni and 13C′i13Ci′. The B1 domain of protein G (GB1), and the enteropathogenic E. coli EspF in complex with human SNX9 SH3, serve as model systems to demonstrate the attainable sensitivity and successful sequential assignment.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofseriesJournal of Biomolecular NMR
dc.rightsCC BY 4.0
dc.subject.otherE. coli
dc.subject.otherEspF
dc.subject.otherGB1
dc.subject.otherintrinsically disordered protein
dc.subject.otherIDP
dc.subject.otherresonance assignment
dc.subject.otherSNX9 SH3
dc.titleHACANCOi : a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202011026466
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosKemian laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.laitosDepartment of Chemistryen
dc.contributor.oppiaineFysikaalinen kemiafi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiainePhysical Chemistryen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange741-752
dc.relation.issn0925-2738
dc.relation.numberinseries12
dc.relation.volume74
dc.type.versionpublishedVersion
dc.rights.copyright© 2020 the Authors
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber288235
dc.subject.ysoNMR-spektroskopia
dc.subject.ysoproteiinit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p26254
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1007/s10858-020-00347-5
dc.relation.funderResearch Council of Finlanden
dc.relation.funderSuomen Akatemiafi
jyx.fundingprogramAcademy Project, AoFen
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundinginformationThis work is supported by the grant from the Academy of Finland (Grant Number 288235 to PP). Open access funding provided by University of Jyväskylä (JYU).
dc.type.okmA1


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