Molecular interactions investigated by multi-dimensional solid-state NMR.
Solid-state NMR (ssNMR) offers insight into the formation of protein complexes and ligand binding for a large range of molecular sizes and binding affinities. Recent instrumental and methodological progress has enabled novel possibilities for using multi-dimensional ssNMR to study molecular 3D structures and interactions in noncrystalline systems. Two-dimensional ssNMR correlation experiments were applied to study ligand binding in globular and membrane proteins and have enabled the investigation of molecular interfaces in the context of protein folding and aggregation. In lipid bilayers, a versatile set of ssNMR experiments has been developed to study molecular structure, topology and complex formation in a functional environment.
Baldus
Marc
M
Max-Planck-Institut für Biophysikalische Chemie, Abteilung für NMR-Basierte Strukturbiologie, 37077 Göttingen, Germany. maba@mpibpc.mpg.de <maba@mpibpc.mpg.de>
D000818:Animals; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D008024:Ligands; D011506:Proteins