High-resolution solid-state NMR applied to polypeptides and membrane proteins.
Solid-state NMR provides unique possibilities to study insoluble or noncrystalline molecules at the atomic level. High-resolution conditions can be established by employing magic-angle spinning at ultrahigh magnetic fields. We discuss NMR methods that make use of these experimental improvements and allow for the study of multiply or uniformly [(13)C,(15)N]-labeled polypeptides and proteins. Recent biophysical applications are reviewed.
Luca
Sorin
S
Department of NMR-Based Structural Biology, Solid-state NMR, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Heise
Henrike
H
Baldus
Marc
M
D008565:Membrane Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
D008565:Membrane Proteins; D010455:Peptides