Statistical averages of hyperfine coupling, g- and zero-field splitting tensors, as well as the p NMR shielding terms, are compared to the available experimental and computational data. We have calculated electron paramagnetic resonance and NMR parameters using quantum-mechanical (QM) computation of molecular dynamics snapshots, obtained using a polarizable empirical force field. More recently, its magnetic properties and also nuclear magnetic relaxation rates have been studied computationally. Ni(2+)(aq) has been used for many decades as a model system for paramagnetic nuclear magnetic resonance (p NMR) relaxation studies. MareÅ¡, Jiřà Hanni, Matti Lantto, Perttu Lounila, Juhani Vaara, Juha Relaxation dispersion difference requires neither selectively labeled samples nor modification of pulse programs thus it will have wide applications in protein dynamics analysis.Ĭurie-type paramagnetic NMR relaxation in the aqueous solution of Ni(II). The results indicate that the structural flexibility of a kink in the heme-binding site is important for efficient heme binding. This new method enabled us to extract exchange parameters from overlapped signals of heme oxygenase-1, which is a relatively large protein. This is the principle of the relaxation dispersion difference method. Therefore, subtraction of each relaxation dispersion spectrum from that with the highest signal intensities, measured at the shortest pulsing interval, leaves only the signals of the fluctuating residues. In relaxation dispersion measurements, the signal intensities of fluctuating residues vary according to the Carr-Purcell-Meiboon-Gill pulsing interval, whereas those of non-fluctuating residues are constant. In this study, we have developed a new methodology called relaxation dispersion difference that can extract conformational exchange parameters from overlapped NMR signals measured using relaxation dispersion spectroscopy. However, signal overlap, which is often observed for such proteins, hampers accurate analysis of NMR data. Recently, NMR has been actively applied to large proteins and intrinsically disordered proteins, which are attractive research targets. NMR is mostly used for investigating such protein dynamics in a site-specific manner. Protein dynamics plays important roles in many biological events, such as ligand binding and enzyme reactions. Konuma, Tsuyoshi Harada, Erisa Sugase, Kenji • Different protein dynamics with different water models.« lessĮxtracting protein dynamics information from overlapped NMR signals using relaxation dispersion difference NMR spectroscopy. • Different protein dynamics with different Histidine charge states in neutral pH. Here, backbone relaxation measurements of ) as common reference between the two methods. However, there exist few reports on correlation analysis between MD and NMR relaxation data. Molecular dynamic (MD) simulations and nuclear magnetic resonance ( NMR) spin relaxation measurements are valuable tools to gain access to fast (nanosecond) internal motions. Internal backbone dynamic motions are essential for different protein functions and occur on a wide range of time scales, from femtoseconds to seconds. General order parameter based correlation analysis of protein backbone motions between experimental NMR relaxation measurements and molecular dynamics simulations
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