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Royal Society of Chemistry, Chemical Communications, 47(51), p. 9624-9627, 2015

DOI: 10.1039/c5cc02685g

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Thioamides in the collagen triple helix

Journal article published in 2015 by Robert W. Newberry ORCID, Brett VanVeller, Ronald T. Raines
This paper is available in a repository.
This paper is available in a repository.

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Abstract

To probe noncovalent interactions within the collagen triple helix, backbone amides were replaced with a thioamide isostere. This subtle substitution is the first in the collagen backbone that does not compromise thermostability. A triple helix with a thioamide as a hydrogen bond donor was found to be more stable than triple helices assembled from isomeric thiopeptides.