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Issue 83, 2013
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Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven

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Abstract

Biophysical and spectroscopic analysis of synthetic transmembrane domain I (TM1) of mycobacteriophage D29 holin shows a lipid concentration dependent conformational switch from an α-helix to a β-sheet structure. The reversibility of this switch, upon change in the lipid-to-peptide ratio, requires a central Pro-Gly segment, and is abolished upon mutation to Ala-Ala or DPro-Gly.

Graphical abstract: Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven

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Publication details

The article was received on 05 Jul 2013, accepted on 20 Aug 2013 and first published on 20 Aug 2013


Article type: Communication
DOI: 10.1039/C3CC45058A
Citation: Chem. Commun., 2013,49, 9594-9596
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    Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven

    M. Lella and R. Mahalakshmi, Chem. Commun., 2013, 49, 9594
    DOI: 10.1039/C3CC45058A

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