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Issue 19, 2016
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Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

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Abstract

We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.

Graphical abstract: Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

  • This article is part of the themed collection: Foldamers
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Publication details

The article was received on 11 Jan 2016, accepted on 02 Feb 2016 and first published on 02 Feb 2016


Article type: Communication
DOI: 10.1039/C6CC00273K
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2016,52, 3789-3792
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    Comparison of design strategies for α-helix backbone modification in a protein tertiary fold

    N. A. Tavenor, Z. E. Reinert, G. A. Lengyel, B. D. Griffith and W. S. Horne, Chem. Commun., 2016, 52, 3789
    DOI: 10.1039/C6CC00273K

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