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European Biophysics Journal

, Volume 36, Supplement 1, pp 37–48 | Cite as

Magnetic resonance in the solid state: applications to protein folding, amyloid fibrils and membrane proteins

  • Marc Baldus
The EBSA prize lecture

Abstract

Solid-state nuclear magnetic resonance (ssNMR) represents a spectroscopic method to study non-crystalline molecules at atomic resolution. Advancements in spectroscopy and biochemistry provide increasing possibilities to study structure and dynamics of complex biomolecular systems by ssNMR. Here, methodological aspects and applications in the context of protein folding and aggregation are discussed. In addition, studies involving membrane proteins are considered.

Keywords

Amyloid Fibril Magic Angle Spin Chemical Shift Anisotropy Anisotropic Interaction Magic Angle Spin Nuclear Magnetic Resonance 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

Work described in this review was supported through grants from the DFG, the FCI, the Volkswagen foundation and the Humboldt foundation, the EU and the Max-Planck Gesellschaft. I thank members of my group and our collaborators over the past 7 years who substantially contributed to work described here. Continuous support by C. Griesinger is gratefully acknowledged.

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Copyright information

© THE EBSA PRIZE LECTURE 2007

Authors and Affiliations

  1. 1.Solid-state NMRMax-Planck-Institut für Biophysikalische ChemieGöttingenGermany

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