NMR spectroscopy occupies a key position in the characterization of biological macromolecules due to its ability to probe dynamic processes and intermolecular interactions with atomic resolution. In the present work, the theory and methodology of NMR techniques for investigations of dynamic processes on fast, pico- to nanosecond, and slow, millisecond time scales are explained. Using these techniques, intrinsic disorder in the helical protrusions of the apical domains of the thermosome with potential implications for substrate binding was revealed. For the nucleotide binding domain of the P-type ATPase Kdp, the effects of AMP-PNP binding on internal motions were investigated. In addition, the optimization of solvent suppression in NMR pulse schemes for use with cryogenic probes is illustrated for selected experiments. Furthermore, solution- and solid-state NMR methods were used to investigate hydrogen bonds in a small cyclic pentapeptide.
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NMR spectroscopy occupies a key position in the characterization of biological macromolecules due to its ability to probe dynamic processes and intermolecular interactions with atomic resolution. In the present work, the theory and methodology of NMR techniques for investigations of dynamic processes on fast, pico- to nanosecond, and slow, millisecond time scales are explained. Using these techniques, intrinsic disorder in the helical protrusions of the apical domains of the thermosome with pote...
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