Abstract
Motions are essential for protein function, and knowledge of protein dynamics is a key to our understanding the mechanisms underlying protein folding and stability, ligand recognition, allostery, and catalysis. In the last two decades, NMR relaxation measurements have become a powerful tool for characterizing backbone and side chain dynamics in complex biological macromolecules such as proteins and nucleic acids. Accurate analysis of the experimental data in terms of motional parameters is an essential prerequisite for developing physical models of motions to paint an adequate picture of protein dynamics. Here, I describe in detail how to use the software package DYNAMICS that was developed for accurate characterization of the overall tumbling and local dynamics in a protein from nuclear spin-relaxation rates measured by NMR. Step-by-step instructions are provided and illustrated through an analysis of 15N relaxation data for protein G.
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Acknowledgments
The development of DYNAMICS program was supported by NIH grant GM 065334. My work on this chapter has led to several modifications of the program, which hopefully made it user-friendlier, and I would like to thank the editors, Alex Shekhtman and David Burz, for being so patient with me during this process.
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Fushman, D. (2012). Determining Protein Dynamics from 15N Relaxation Data by Using DYNAMICS. In: Shekhtman, A., Burz, D. (eds) Protein NMR Techniques. Methods in Molecular Biology, vol 831. Humana Press. https://doi.org/10.1007/978-1-61779-480-3_24
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DOI: https://doi.org/10.1007/978-1-61779-480-3_24
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