Magnetic resonance in the solid state: applications to protein folding, amyloid fibrils and membrane proteins
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.
KeywordsAmyloid Fibril Magic Angle Spin Chemical Shift Anisotropy Anisotropic Interaction Magic Angle Spin Nuclear Magnetic Resonance
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.
- Cavanagh J, Fairbrother WJ, Palmer AG, Skelton NJ (1996) Protein NMR spectroscopy, principles and practice. Academic, San DiegoGoogle Scholar
- Coutant J, Curmi PA, Toma F, Monti JP (2007) NMR solution structure of neurotensin in membrane-mimetic environments: molecular basis for neurotensin receptor recognition. Biochemistry (in press)Google Scholar
- Ernst RR, Bodenhausen G, Wokaun A (1987) Principles of nuclear magnetic resonance in one and two dimensions. Clarendon, OxfordGoogle Scholar
- Grisshammer R, Tucker J (2000) Expression in Escherichia coli and large-scale purification of a rat neurotensin receptor. In: Haga T, Bernstein G (eds) G protein coupled receptors. CRC, Boca Raton, pp 265–280Google Scholar
- Heise H, Hoyer W, Becker S, Seidel K, Baldus M (2007) Fibril topology of full-length a-synuclein probed by solid-state NMR spectroscopy (submitted)Google Scholar
- Schneider R, Etzkorn M, Baldus M (2007) Molecular motion detected by double-quantum (13C,13C) solid-state NMR spectroscopy (submitted)Google Scholar
- Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R (1995) A prokaryotic potassium-ion channel with 2 predicted transmembrane segments from Streptomyces lividans. EMBO J 14:5170–5178Google Scholar
- Seidel K, Lange A, Becker S, Hughes CE, Heise H, Baldus M (2004) Protein solid-state NMR resonance assignments from (13C,13C) correlation spectroscopy. PhysChemChemPhys 6:5090–5093Google Scholar
- Wüthrich K (1986) NMR of proteins and nucleic acids. Wiley Interscience, New YorkGoogle Scholar