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PMID: 2553484 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 257 ·No. 1 ·1989-10-23 ·Pages 113-7

Mulvey D, King GF, Cooke RM, Doak DG, Harvey TS, Campbell ID

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.

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

Chemicals

Membrane Proteins Peptide Fragments Sodium Channels Hydrogen

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Mulvey D

Department of Biochemistry, University of Oxford, England.

King G F

Cooke R M

Doak D G

Harvey T S

Campbell I D

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(89)81799-5

Published

1989-10-23

Pages

113-7

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(89)81799-5 View journal details

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

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