Ontology highlight
ABSTRACT:
SUBMITTER: Newberry RW
PROVIDER: S-EPMC4449287 | biostudies-literature | 2015 Jun
REPOSITORIES: biostudies-literature
Chemical communications (Cambridge, England) 20150601 47
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. ...[more]