High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein

D Mulvey; G F King; R M Cooke; D G Doak; T S Harvey; I D Campbell

doi:10.1016/0014-5793(89)81799-5

High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein

FEBS Lett. 1989 Oct 23;257(1):113-7. doi: 10.1016/0014-5793(89)81799-5.

Authors

D Mulvey¹, G F King, R M Cooke, D G Doak, T S Harvey, I D Campbell

Affiliation

¹ Department of Biochemistry, University of Oxford, England.

PMID: 2553484
DOI: 10.1016/0014-5793(89)81799-5

Abstract

A peptide (S4) of the rat brain sodium channel has been synthesized, studied by high-resolution NMR and its secondary structure modelled by distance geometry and restrained molecular dynamics techniques.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Hydrogen
Magnetic Resonance Spectroscopy / methods
Membrane Proteins* / isolation & purification
Models, Molecular
Molecular Sequence Data
Peptide Fragments* / chemical synthesis
Protein Conformation
Sodium Channels / analysis*

Substances

Membrane Proteins
Peptide Fragments
Sodium Channels
Hydrogen