title: Thioamides in the collagen triple helix.
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.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706-1322, USA. rtraines@wisc.edu.
authors.forename: Robert W
authors.initials: RW
authors.lastname: Newberry
authors.forename: Brett
authors.initials: B
authors.lastname: VanVeller
authors.forename: Ronald T
authors.initials: RT
authors.lastname: Raines
mesh_terms: D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D019277:Entropy; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013854:Thioamides / Q000737:chemistry*
chemical_list: D013854:Thioamides; D003094:Collagen