Peptide structural analysis by solid-state NMR spectroscopy

Solid-state nmr spectroscopy provides a robust method for investigating pol ypeptides that have been prepared by chemical synthesis and that are immobi lized by strong interactions with solid surfaces or large macroscopic compl exes. Solid-state nmr spectroscopy has been widely used to investigate memb rane polypeptides or peptide aggregates such as amyloid fibrils. Whereas ma gic angle spinning solid-state nmr spectroscopy allows one to measure dista nces and dihedral angles with high accuracy, static membrane samples that a re aligned with respect to the magnetic field direction allow one to determ ine the secondary structure of bound polypeptides and their orientation wit h respect to the bilayer normal. Peptide dynamics and the effect of polypep tides on the macroscopic phase preference of phospholipid membranes have be en investigated in nonoriented samples. Investigations of the structure and topology of membrane channels, peptide antibiotics, signal sequences as we ll as model systems that allow one to dissect the interaction contributions irt phospholipid membranes will be presented in greater detail. (C) 1999 J ohn Wiley & Sons, Inc.