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Detection and Analysis of Chimeric Tertiary Structures by Backbone Thioester Exchange: Packing of an α Helix against an α/β-Peptide Helix

Authors

  • Joshua L. Price,

    1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA), Fax: (+1) 608-265-4534
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    • These authors contributed equally.

  • Erik B. Hadley,

    1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA), Fax: (+1) 608-265-4534
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    • These authors contributed equally.

  • Jay D. Steinkruger,

    1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA), Fax: (+1) 608-265-4534
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  • Samuel H. Gellman Prof. Dr.

    1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA), Fax: (+1) 608-265-4534
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  • This research was supported by the NIH Grant GM-61238. J.L.P. was supported in part by an NIH Chemical Biology Training Grant (T32 GM008505). We thank Dr. Darrell McCaslin for assistance with AU experiments, and Peptech for providing β3-amino acids at a discounted price.

Abstract

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Backbone thioester exchange is used to explore a fundamental type of protein–foldamer packing motif, the association of an α helix and an α/β-peptide foldameric helix, which is analogous to an antiparallel coiled-coil tertiary structure in a pure α-residue backbone. Side-chain packing preferences at this chimeric tertiary interface are comparable to those that determine pairing propensities among antiparallel α helices.

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