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Issue 43, 2013
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Circular permutation of the Trp-cage: fold rescue upon addition of a hydrophobic staple

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Abstract

The Trp-cage, at 20 residues in length, is generally acknowledged as the smallest fully protein-like folding motif. Linking the termini by a two-residue unit and excising one residue affords circularly permuted sequences that adopt the same structure. This represents the first successful circular permutation of any fold of less than 50-residue length. As was observed for the original topology, a hydrophobic staple near the chain termini is required for enhanced fold stability.

Graphical abstract: Circular permutation of the Trp-cage: fold rescue upon addition of a hydrophobic staple

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Publication details

The article was received on 16 Jul 2013, accepted on 20 Aug 2013 and first published on 02 Sep 2013


Article type: Communication
DOI: 10.1039/C3RA43674H
Citation: RSC Adv., 2013,3, 19824-19829
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    Circular permutation of the Trp-cage: fold rescue upon addition of a hydrophobic staple

    A. Byrne, B. L. Kier, D. V. Williams, M. Scian and N. H. Andersen, RSC Adv., 2013, 3, 19824
    DOI: 10.1039/C3RA43674H

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