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Issue 12, 2015
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p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore–quencher pair for short distance measurements: application to polyproline peptides

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Abstract

The C[triple bond, length as m-dash]N stretching frequency and fluorescence quantum yield of p-cyanophenylalanine are sensitive to environment. As such, this unnatural amino acid has found broad applications, ranging from studying how proteins fold to determining the local electric field of membranes. Herein, we demonstrate that the fluorescence of p-cyanophenylalanine can be quenched by selenomethionine through an electron transfer process occurring at short distances, thus further expanding its spectroscopic utility. Using this fluorophore–quencher pair, we are able to show that short polyproline peptides (1–4 prolines) are not rigid; instead, they sample a bimodal conformational distribution.

Graphical abstract: p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore–quencher pair for short distance measurements: application to polyproline peptides

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Publication details

The article was received on 05 Jan 2015, accepted on 19 Feb 2015 and first published on 20 Feb 2015


Article type: Paper
DOI: 10.1039/C5CP00050E
Citation: Phys. Chem. Chem. Phys., 2015,17, 7881-7887
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    p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore–quencher pair for short distance measurements: application to polyproline peptides

    M. R. Mintzer, T. Troxler and F. Gai, Phys. Chem. Chem. Phys., 2015, 17, 7881
    DOI: 10.1039/C5CP00050E

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