Cis-peptide bonds are rare in proteins, and building blocks less favorable to the trans-
conformer have been considered destabilizing. Although proline tolerates the cis-conformer …

As the only ribosomally encoded N-substituted amino acid, proline promotes distinct
secondary protein structures. The high proline content in collagen, the most abundant …

Collagen mimetic peptides (CMPs) fold into a polyproline type II triple helix, allowing the
study of the structure and function (or misfunction) of the collagen family of proteins. This …

Nearly 30% of human proteins have tandem repeating sequences. Structural understanding
of the terminal repeats is well-established for many repeat proteins with the common α-helix …

Collagen model peptides (CMPs) serve as tools for understanding stability and function of
the collagen triple helix and have a potential for biomedical applications. In the past …

Natural interruptions in the repeating (Gly-XY) n amino acid sequence pattern are found
normally in triple helix domains of all nonfibrillar collagens, while any Gly substitution in …

Mismatch is fine: Proline derivatives with a ring pucker mismatching that of natural collagen
but with favorable torsional angles along the peptide chain are readily tolerated within the …

Collagen mimics are peptides designed to reproduce structural features of natural collagen.
A triple helix is the first element in the hierarchy of collagen folding. It is an assembly of three …

Collagen model peptides (CMPs), composed of proline–(2 S, 4 R)-hydroxyproline–glycine
(POG) repeat units, have been extensively used to study the structure and stability of triple …

We investigated the effect of restricting cis− trans proline isomerization on collagen triple-
helix stability. The Pro residues at the Xaa and Yaa positions of an (Xaa-Yaa-Gly) triplet …