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A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities

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dc.abstract.enIntrinsically disordered proteins (IDPs) are challenging established structural biology perception and urge a reassessment of the conventional understanding of the subtle interplay between protein structure and dynamics. Due to their importance in eukaryotic life and central role in protein interaction networks, IDP research is a fascinating and highly relevant research area in which NMR spectroscopy is destined to be a key player. The flexible nature of IDPs, as a result of the sampling of a vast conformational space, however, poses a tremendous scientific challenge, both technically and theoretically. Pronounced signal averaging results in narrow signal dispersion and requires higher dimensionality NMR techniques. Moreover, a fundamental problem in the structural characterization of IDPs is the definition of the conformational ensemble sampled by the polypeptide chain in solution, where often the interpretation relies on the concept of ‘residual structure’ or ‘conformational preference’. An important source of structural information is information-rich NMR experiments that probe protein backbone dihedral angles in a unique manner. Cross-correlated relaxation experiments have proven to fulfil this task as they provide unique information about protein backbones, particularly in IDPs. Here we present a novel cross-correlation experiment that utilizes non-uniform sampling detection schemes to resolve protein backbone dihedral ambiguities in IDPs. The sensitivity of this novel technique is illustrated with an application to the prototypical IDP -Synculein for which unexpected deviations from random-coil-like behaviour could be observed.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorZawadzka-Kazimierczuk, Anna
dc.contributor.authorKauffmann, Clemens
dc.contributor.authorSchwarz, Thomas C.
dc.contributor.authorKonrat, Robert
dc.contributor.authorKazimierczuk, Krzysztof
dc.date.accessioned2024-01-24T18:04:40Z
dc.date.available2024-01-24T18:04:40Z
dc.date.copyright2020-04-01
dc.date.issued2020
dc.description.accesstimeAT_PUBLICATION
dc.description.financePublikacja bezkosztowa
dc.description.number4-5
dc.description.versionFINAL_PUBLISHED
dc.description.volume74
dc.identifier.doi10.1007/S10858-020-00308-Y
dc.identifier.issn0925-2738
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/101764
dc.identifier.weblinkhttp://link.springer.com/content/pdf/10.1007/s10858-020-00308-y.pdf
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofJournal of Biomolecular NMR
dc.relation.pages257-265
dc.rightsCC-BY
dc.sciencecloudnosend
dc.subject.enCross-correlated relaxation
dc.subject.enDihedral angles
dc.subject.enChemical shift anisotropy
dc.subject.enDipolar interactions
dc.subject.enIntrinsically disordered proteins
dc.subject.enHigh-dimensional NMR experiments
dc.subject.enNon-uniform sampling
dc.titleA novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities
dc.typeJournalArticle
dspace.entity.typePublication