Abstract
Solid-state NMR (ssNMR) provides increasing possibilities to study structure and dynamics of biomolecular systems. Our group has been interested in developing ssNMR-based approaches that are applicable to biomolecules of increasing molecular size and complexity without the need of specific isotope-labelling. Methodological aspects ranging from spectral assignments to the indirect detection of proton–proton contacts in multi-dimensional ssNMR are discussed and applied to (membrane) protein complexes.
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Acknowledgments
Work described in this review was supported through grants from the Deutsche Forschungsgemeinschaft (DFG), the Fonds der Chemischen Industrie (FCI), the Volkswagen foundation, the Humboldt foundation, the EU and the Max-Planck-Gesellschaft. I thank all group members, our colleagues and collaborators over the past years who substantially contributed to work described here. Most experiments described here were conducted in the department of NMR-based Structural Biology headed by C. Griesinger. I am indebted to the International Council on Magnetic in Biological Systems for awarding me the founder’s medal 2006. While this article exclusively discussed results obtained in our group, progress in the field was only possible due to the outstanding contributions of many other groups and colleagues.
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Baldus, M. ICMRBS founder’s medal 2006: Biological solid-state NMR, methods and applications. J Biomol NMR 39, 73–86 (2007). https://doi.org/10.1007/s10858-007-9177-3
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DOI: https://doi.org/10.1007/s10858-007-9177-3