Characterisation of protein structure and dynamics by NMR spectroscopy and computational methods

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dc.contributor.advisorLinser, Rasmus
dc.contributor.authorSöldner, Benedikt
dc.contributor.refereeSchäfer, Lars
dc.date.accepted2025-11-24
dc.date.accessioned2026-01-12T14:27:32Z
dc.date.available2026-01-12T14:27:32Z
dc.date.issued2025
dc.description.abstractNuclear magnetic resonance (NMR) spectroscopy is a powerful technique for studying the structure and dynamics of proteins. In contrast to almost all other experimental techniques, NMR spectroscopy facilitates the elucidation of site-specific protein dynamics on various timescales, making it an indispensable tool for structural biology of proteins. In the first chapter, the theory of NMR spectroscopy is introduced and an overview of frequently used NMR spectroscopic methods for studying protein structure and dynamics is given. In addition, an introduction about molecular dynamics (MD) simulations, a technique for studying protein dynamics on an atomic scale used for explaining the dynamics detected by NMR spectroscopy as well as constituting a technique for structure determination of proteins based on observables from NMR spectroscopy, is given. In chapter 2 – 5, the four major projects investigated for my Ph. D. are presented. In chapter 2, a newly developed method for determining accurate distances from 1H-detected solid-state NMR spectroscopy is presented and demonstrated by structure determination and restrained MD simulations of the chicken α-spectrin SH3 domain. In the project presented in chapter 3, microsecond-timescale dynamics of a small-molecule ligand bound to the active site of the human carbonic anhydrase II (hCAII) was revealed with solid-state NMR spectroscopy, where my contribution consisted in determining the origin of the dynamics on an atomic level using MD simulations. In the project shown in chapter 4, the influence of salt concentration on the protein dynamics was investigated by NMR spectroscopy and MD simulations. In the project presented in chapter 5, the secondary-messenger-induced allosteric modulation of conformational loop dynamics in the PII-like protein A (PstA) is investigated. In addition to the modulation of the spatial properties of the 30-residue long loops, in absence of the ligand, also slow µs-ms timescale dynamics in the core of PstA are revealed.en
dc.identifier.urihttp://hdl.handle.net/2003/44666
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-26434
dc.language.isoen
dc.subjectNuclear magnetic resonance spectroscopyen
dc.subjectProtein dynamicsen
dc.subjectProtein Complexesen
dc.subjectSolid-State NMRen
dc.subjectMolecular dynamicsen
dc.subjectIntegrated structural biologyen
dc.subject.ddc540
dc.subject.rswkNMR-Spektroskopiede
dc.subject.rswkMultiproteinkomplexde
dc.subject.rswkFestkörper-NMR-Spektroskopiede
dc.subject.rswkMolekulardynamikde
dc.subject.rswkProteinede
dc.subject.rswkStrukturbiologiede
dc.subject.rswkMolekülstrukturde
dc.subject.rswkComputerunterstütztes Verfahrende
dc.titleCharacterisation of protein structure and dynamics by NMR spectroscopy and computational methodsen
dc.typeText
dc.type.publicationtypePhDThesis
dcterms.accessRightsopen access
eldorado.dnb.deposittrue
eldorado.secondarypublicationfalse

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Physikalische Chemie