1. Peptide structural analysis by solid-state NMR spectroscopy
- Author
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Burkhard Bechinger, Titus C. B. Vogt, Rudolf Kinder, Susan Schinzel, Ulrike Harzer, and Michael Helmle
- Subjects
Models, Molecular ,Magnetic Resonance Spectroscopy ,Nitrogen Isotopes ,Chemistry ,Bilayer ,Organic Chemistry ,Biophysics ,Membrane Proteins ,Phosphorus ,General Medicine ,Nuclear magnetic resonance spectroscopy ,Hydrogen-Ion Concentration ,Dihedral angle ,Biochemistry ,Ion Channels ,Anti-Bacterial Agents ,Biomaterials ,Crystallography ,Membrane ,Solid-state nuclear magnetic resonance ,Magic angle spinning ,Peptides ,Spectroscopy ,Protein secondary structure ,Hydrogen - Abstract
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. © 1999 John Wiley & Sons, Inc. Biopoly 51: 174–190, 1999
- Published
- 1999