Literature DB >> 2478193

Effect of acyl chain length on the structure and motion of gramicidin A in lipid bilayers.

B A Cornell1, F Separovic, D E Thomas, A R Atkins, R Smith.   

Abstract

The transmembrane ion transport properties of gramicidin A have previously been shown to dependent on the nature of its lipid environment. Solid-state NMR spectroscopic studies of 13C-labelled analogues of gramicidin in oriented multilayers of phosphatidylcholine have shown that variation of the lipid hydrocarbon chain length has no effect on the structure or orientation of the peptide backbone.

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Year:  1989        PMID: 2478193     DOI: 10.1016/0005-2736(89)90368-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Modulation of concentration fluctuations in phase-separated lipid membranes by polypeptide insertion.

Authors:  S Fahsel; E-M Pospiech; M Zein; T L Hazlet; E Gratton; Roland Winter
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

2.  Solid-state C NMR spectroscopy of a C carbonyl-labeled polypeptide.

Authors:  C Wang; Q Teng; T A Cross
Journal:  Biophys J       Date:  1992-06       Impact factor: 4.033

3.  A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering.

Authors:  T Heimburg; R L Biltonen
Journal:  Biophys J       Date:  1996-01       Impact factor: 4.033

4.  Alpha-helical hydrophobic polypeptides form proton-selective channels in lipid bilayers.

Authors:  A E Oliver; D W Deamer
Journal:  Biophys J       Date:  1994-05       Impact factor: 4.033

5.  Monitoring gramicidin conformations in membranes: a fluorescence approach.

Authors:  Satinder S Rawat; Devaki A Kelkar; Amitabha Chattopadhyay
Journal:  Biophys J       Date:  2004-08       Impact factor: 4.033

  5 in total

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