Publisher Summary Turns are a fundamental class of polypeptide structure and are defined
as sites where the peptide chain reverses its overall direction. In the past 20 years, the …

The molecular conformation of the collagen triple helix confers strict amino acid sequence
constraints, requiring a (Gly-XY) n repeating pattern and a high content of imino acids. The …

Publisher Summary The chapter discusses the protein stability with emphasis on compact
globular proteins representing a single cooperative system. All the small compact globular …

Background: The collagen triple helix is a unique protein motif defined by the supercoiling of
three polypeptide chains in a polyproline II conformation. It is a major domain of all collagen …

Astructure was proposed for collagen by us about a year ago1• Although it explains the
features of the infra-red spectrum and the chemical composition of collagen, it appears to be …

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 …

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 …

This paper reviews the ultrastructure and chemistry of fish bone, with an emphasis on
zooarchaeology and stable isotope analysis. On the basis of the chemical composition of the …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Aim and methods Collagen is the most abundant protein found in animal body, which is
widely used for biomedical and pharmaceutical applications. In the present study, acid …