Abstract
Based on a tremendous technological progress, during the past decade it has been demonstrated that solid-state NMR is capable of providing very detailed information about the structure and dynamics of biological molecules in the solid phase. Using state-of-the-art methodology, it is now realistic to resolve, assign, and structurally interpret resonances from peptides/proteins with about 50 – 100 residues and to obtain local structure information for proteins an order of magnitude larger. With considerable room for future development (higher magnetic fields, stronger rf fields, higher spinning speeds, new isotope labeling and expression methods, and new multi-dimensional pulse sequences), these achievements open up exiting perspectives for the study of, e.g., membrane proteins, protein aggregates, and colloids. This is of great importance considering that, e.g., membrane proteins in one way or another are involved in most biological processes and simultaneously may be extremely difficult to characterize at atomic resolution using traditional structure determination methods.
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Bak, M., Schultz, R., Nielsen, N.C. (2001). Numerical simulations for experiment design and extraction of structural parameters in biological solid-state NMR spectroscopy. In: Kiihne, S.R., de Groot, H.J.M. (eds) Perspectives on Solid State NMR in Biology. Focus on Structural Biology, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2579-8_9
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DOI: https://doi.org/10.1007/978-94-017-2579-8_9
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