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Issue 23, 2008
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Hyperstable miniproteins: additive effects of D- and L-Ala mutations

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Abstract

The folding enantioselectivity for D-AlaversusL-Ala at one glycine site in the Trp-cage is 16 kJ mol−1; judicious introductions of alanines of the correct chirality raises the melting temperature of this 20-residue fold to 83 °C.

Graphical abstract: Hyperstable miniproteins: additive effects of d- and l-Ala mutations

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Publication details

The article was received on 18 Aug 2008, accepted on 25 Sep 2008 and first published on 15 Oct 2008


Article type: Communication
DOI: 10.1039/B814314E
Citation: Org. Biomol. Chem., 2008,6, 4287-4289
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    Hyperstable miniproteins: additive effects of D- and L-Ala mutations

    D. V. Williams, B. Barua and N. H. Andersen, Org. Biomol. Chem., 2008, 6, 4287
    DOI: 10.1039/B814314E

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