Peptide structural analysis by solid-state NMR spectroscopy

✍ Scribed by Burkhard Bechinger; Rudolf Kinder; Michael Helmle; Titus C. B. Vogt; Ulrike Harzer; Susan Schinzel

• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 185 KB
• Volume: 51
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(1999)51:3<174::aid-bip2>3.0.co;2-7

✦ Synopsis

Solid-state nmr spectroscopy provides a robust method for investigating polypeptides that have been prepared by chemical synthesis and that are immobilized by strong interactions with solid surfaces or large macroscopic complexes. Solid-state nmr spectroscopy has been widely used to investigate membrane polypeptides or peptide aggregates such as amyloid fibrils. Whereas magic angle spinning solid-state nmr spectroscopy allows one to measure distances and dihedral angles with high accuracy, static membrane samples that are aligned with respect to the magnetic field direction allow one to determine the secondary structure of bound polypeptides and their orientation with respect to the bilayer normal. Peptide dynamics and the effect of polypeptides on the macroscopic phase preference of phospholipid membranes have been investigated in nonoriented samples. Investigations of the structure and topology of membrane channels, peptide antibiotics, signal sequences as well as model systems that allow one to dissect the interaction contributions in phospholipid membranes will be presented in greater detail.