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.
Baldus
Marc
M
Solid-state NMR, Max-Planck-Institut für Biophysikalische Chemie, 37077 Göttingen, Germany. maba@mpibpc.mpg.de
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding
D000682:Amyloid; D008565:Membrane Proteins