Abstract
High-resolution NMR spectroscopy has become a unique and powerful approach with atomic resolution not only for determining structures of biological macromolecules but also for characterizing the overall and internal rotational motions in proteins. The dynamic behavior of proteins at different timescales can be monitored experimentally by different methods because it is difficult, if not impossible, to completely characterize all motional processes by a single approach. Nuclear spin relaxation measurement provides information on fast motions on the timescales of picosecond to nanosecond (laboratory frame nuclear spin relaxation experiments), and slow motions on the timescales of microsecond to millisecond (rotating frame nuclear spin relaxation measurements), whereas magnetization exchange spectroscopy deals with motions on the timescales of millisecond to second. This chapter focuses on the experiments and data analysis for heteronuclear spin relaxation approaches used to characterize the dynamic processes of proteins in solution.
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Teng, Q. (2013). Protein Dynamics. In: Structural Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-3964-6_8
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DOI: https://doi.org/10.1007/978-1-4614-3964-6_8
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