The main features of the triple helical structure of collagen were deduced in the mid-1950s
from fibre X-ray diffraction of tendons. Yet, the resulting models only could offer an average …

Publisher Summary Protein folding is a process by which a polypeptide chain acquires its
native structure from an unfolded state through a transition state. Recent studies of the …

Sequence dependent conformational variations of collagen triple-helical structure | Nature
Structural & Molecular Biology Skip to main content Thank you for visiting nature.com. You are …

The applicability of the newly developed PM6 method for modeling proteins is investigated.
In order to allow the geometries of such large systems to be optimized rapidly, three …

The first report of the full‐length structure of the collagen‐like polypeptide [(Pro‐Pro‐Gly) 10]
3 is given. This structure was obtained from crystals grown in a microgravity environment …

Collagen-like peptides of the type (Pro-Pro-Gly) 10 fold into stable triple helices. An electron-
withdrawing substituent at the Hγ3 ring position of the second proline residue stabilizes …

Collagen is the most abundant protein in animals and the major component of connective
tissues. Although collagen isolated from natural sources has long served as the basis for …

This year marks the 50th anniversary of the coiled?‐? coil triple helical structure of collagen,
first proposed by Ramachandran's group from Madras. The structure is unique among the …

The collagen triple helix is a widespread structural element, which not only occurs in
collagens but also in many other proteins. The triple helix consists of three identical or …

Under eons of evolutionary and environmental pressure, biological systems have developed
strong and lightweight peptide‐based polymeric materials by using the 20 naturally …