Peptide structural analysis by solid-state NMR spectroscopy.

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.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Bechinger B,Kinder R,Helmle M,Vogt TC,Harzer U,Schinzel S

doi

10.1002/(SICI)1097-0282(1999)51:3<174::AID-BIP2>3.

subject

Has Abstract

pub_date

1999-01-01 00:00:00

pages

174-90

issue

3

eissn

0006-3525

issn

1097-0282

pii

10.1002/(SICI)1097-0282(1999)51:3<174::AID-BIP2>3.

journal_volume

51

pub_type

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