Abstract
Solid-state NMR has become the method of choice for the assessment of protein structure for insoluble objects lacking long-range order. In this context, it is apparent that solid-state NMR is also perfectly poised toward the characterization of immobilized proteins. For these systems, it is possible to understand at the atomic level which perturbations, if any, are occurring as a result of the functionalization. Here we describe how it is possible to accomplish the NMR characterization of enzymes that have been immobilized through different approaches, and we introduce the reader to the choice of the experimental strategy that can be useful in different cases. An outlook on the level of information that can be attained is also given, in view of recent methodological advancements.
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Acknowledgments
Dr. Venita Decker and Dr. Sebastian Wegner (Bruker Biospin), and Dr. Yusuke Nishiyiama (JEOL) are acknowledged for providing the instructions for operating low-diameter rotors.
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Cerofolini, L., Ravera, E., Fragai, M., Luchinat, C. (2020). NMR of Immobilized Enzymes. In: Guisan, J., Bolivar, J., López-Gallego, F., Rocha-MartÃn, J. (eds) Immobilization of Enzymes and Cells. Methods in Molecular Biology, vol 2100. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0215-7_24
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