001042312 001__ 1042312
001042312 005__ 20250804115244.0
001042312 0247_ $$2doi$$a10.1021/jacs.5c04159
001042312 0247_ $$2ISSN$$a0002-7863
001042312 0247_ $$2ISSN$$a1520-5126
001042312 0247_ $$2ISSN$$a1943-2984
001042312 0247_ $$2datacite_doi$$a10.34734/FZJ-2025-02519
001042312 0247_ $$2pmid$$a40285725
001042312 0247_ $$2WOS$$aWOS:001477553300001
001042312 037__ $$aFZJ-2025-02519
001042312 082__ $$a540
001042312 1001_ $$0P:(DE-Juel1)198708$$aLevorin, Leonardo$$b0
001042312 245__ $$aIsoleucine Side Chains as Reporters of Conformational Freedom in Protein Folding Studied by DNP-Enhanced NMR
001042312 260__ $$aWashington, DC$$bACS Publications$$c2025
001042312 3367_ $$2DRIVER$$aarticle
001042312 3367_ $$2DataCite$$aOutput Types/Journal article
001042312 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1750917357_29661
001042312 3367_ $$2BibTeX$$aARTICLE
001042312 3367_ $$2ORCID$$aJOURNAL_ARTICLE
001042312 3367_ $$00$$2EndNote$$aJournal Article
001042312 520__ $$aConformations of protein side chains are closely linked to protein function. DNP-enhanced solid-state NMR (ssNMR), which operates at cryogenic temperatures (<110 K), can be used to freeze-trap protein conformations, including the side chains. In the present study, we employed two-dimensional DNP-enhanced ssNMR to get detailed insights into backbone and side chain conformations of isoleucine. We used different amino acid selectively labeled model proteins for intrinsically disordered proteins (IDPs), denatured and well-folded proteins, and amyloid fibrils. 13C chemical shifts are closely correlated with secondary structure elements and χ1 and χ2 angles in isoleucine side chains. Thus, line shape analysis by integration of representative peak areas in 2D spectra provides an accurate overview of the distribution of backbone and side chain conformations. For the well-folded proteins GABARAP and bovine PI3-kinase (PI3K) SH3 domain, most Ile chemical shifts in frozen solution are well resolved and similar to those observed in solution. However, line widths of individual Ile residues are directly linked to residual mobility, and line broadening or even signal splitting appears for those Ile residues, which are not part of well-defined secondary structure elements. For unfolded PI3K SH3 and the IDP α-synuclein (α-syn), all Ile side chains have full conformational freedom, and as a consequence, inhomogeneous line broadening dominates the cryogenic spectra. Moreover, we demonstrate that conformational ensembles of proteins strongly depend on solvent and buffer conditions. This allowed different unfolded structures for chemical and acidic pH denaturation of the PI3K SH3 domain to be distinguished. In amyloid fibrils of α-syn and PI3K SH3, chemical shifts typical for β-strand like secondary structure dominate the spectra, whereas Ile residues belonging to the fuzzy coat still add the IDP-type line shapes. Hence, DNP-enhanced ssNMR is a useful tool for investigating side chain facilitated protein functions and interactions.
001042312 536__ $$0G:(DE-HGF)POF4-5244$$a5244 - Information Processing in Neuronal Networks (POF4-524)$$cPOF4-524$$fPOF IV$$x0
001042312 588__ $$aDataset connected to CrossRef, Journals: juser.fz-juelich.de
001042312 7001_ $$0P:(DE-Juel1)178027$$aBecker, Nina$$b1
001042312 7001_ $$0P:(DE-Juel1)208937$$aUluca-Yazgi, Boran$$b2$$ufzj
001042312 7001_ $$0P:(DE-Juel1)185029$$aGardon, Luis$$b3
001042312 7001_ $$0P:(DE-Juel1)190543$$aKraus, Mirko$$b4
001042312 7001_ $$0P:(DE-Juel1)165152$$aSevenich, Marc$$b5
001042312 7001_ $$0P:(DE-HGF)0$$aApostolidis, Athina$$b6
001042312 7001_ $$0P:(DE-HGF)0$$aSchmitz, Kai$$b7
001042312 7001_ $$0P:(DE-Juel1)201187$$aRüter, Neomi$$b8
001042312 7001_ $$0P:(DE-Juel1)172053$$aApanasenko, Irina$$b9
001042312 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b10
001042312 7001_ $$0P:(DE-Juel1)201143$$aHoyer, Wolfgang$$b11$$ufzj
001042312 7001_ $$0P:(DE-Juel1)144510$$aNeudecker, Philipp$$b12
001042312 7001_ $$0P:(DE-Juel1)145165$$aGremer, Lothar$$b13
001042312 7001_ $$0P:(DE-Juel1)132002$$aHeise, Henrike$$b14$$eCorresponding author
001042312 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/jacs.5c04159$$gVol. 147, no. 18, p. 15867 - 15879$$n18$$p15867 - 15879$$tJournal of the American Chemical Society$$v147$$x0002-7863$$y2025
001042312 8564_ $$uhttps://juser.fz-juelich.de/record/1042312/files/levorin-et-al-2025-isoleucine-side-chains-as-reporters-of-conformational-freedom-in-protein-folding-studied-by-dnp.pdf$$yOpenAccess
001042312 8767_ $$d2025-05-12$$eHybrid-OA$$jPublish and Read
001042312 909CO $$ooai:juser.fz-juelich.de:1042312$$pdnbdelivery$$popenCost$$pVDB$$pdriver$$popen_access$$popenaire
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)198708$$aForschungszentrum Jülich$$b0$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)208937$$aForschungszentrum Jülich$$b2$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)185029$$aForschungszentrum Jülich$$b3$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)190543$$aForschungszentrum Jülich$$b4$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)172053$$aForschungszentrum Jülich$$b9$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132029$$aForschungszentrum Jülich$$b10$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)201143$$aForschungszentrum Jülich$$b11$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)144510$$aForschungszentrum Jülich$$b12$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)145165$$aForschungszentrum Jülich$$b13$$kFZJ
001042312 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132002$$aForschungszentrum Jülich$$b14$$kFZJ
001042312 9131_ $$0G:(DE-HGF)POF4-524$$1G:(DE-HGF)POF4-520$$2G:(DE-HGF)POF4-500$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$9G:(DE-HGF)POF4-5244$$aDE-HGF$$bKey Technologies$$lNatural, Artificial and Cognitive Information Processing$$vMolecular and Cellular Information Processing$$x0
001042312 9141_ $$y2025
001042312 915pc $$0PC:(DE-HGF)0000$$2APC$$aAPC keys set
001042312 915pc $$0PC:(DE-HGF)0122$$2APC$$aHelmholtz: American Chemical Society 01/01/2023
001042312 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0160$$2StatID$$aDBCoverage$$bEssential Science Indicators$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1190$$2StatID$$aDBCoverage$$bBiological Abstracts$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)9915$$2StatID$$aIF >= 15$$bJ AM CHEM SOC : 2022$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ AM CHEM SOC : 2022$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1210$$2StatID$$aDBCoverage$$bIndex Chemicus$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0113$$2StatID$$aWoS$$bScience Citation Index Expanded$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
001042312 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1150$$2StatID$$aDBCoverage$$bCurrent Contents - Physical, Chemical and Earth Sciences$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)1200$$2StatID$$aDBCoverage$$bChemical Reactions$$d2024-12-13
001042312 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2024-12-13
001042312 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
001042312 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz$$d2024-12-13$$wger
001042312 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List$$d2024-12-13
001042312 920__ $$lyes
001042312 9201_ $$0I:(DE-Juel1)IBI-7-20200312$$kIBI-7$$lStrukturbiochemie$$x0
001042312 980__ $$ajournal
001042312 980__ $$aVDB
001042312 980__ $$aUNRESTRICTED
001042312 980__ $$aI:(DE-Juel1)IBI-7-20200312
001042312 980__ $$aAPC
001042312 9801_ $$aAPC
001042312 9801_ $$aFullTexts