The Structure of Collagen

  title={The Structure of Collagen},
  author={Alexander Rich and Francis H. C. Crick},
During the 1950s Crick made crucial contributions not only to the study of DNA and the genetic code, but to X-ray structure analysis of important biological molecules. He was instrumental in extending helical diffraction theory to construct three-dimensional maps of protein molecules from X-ray data. In particular, he calculated the complicated X-ray diffraction pattern produced by a helix that was itself wound around a second axis into a larger super helix, or coiled coil. In this paper… 
The structure of collagen.
The different genetic types of collagen, and the structure of the triple-helical molecule as refined from X-ray fibre diffraction data, are described and an account is given of the quasi-hexagonal model.
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
The structure of a protein triple helix has been determined by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence, which adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen.
Stereochemistry of collagen.
Almost all features of the primary structure, X-ray pattern, optical and hydrodynamic data, and the role of hydroxyproline in stabilising the triple helical structure, have been satisfactorily accounted for and lead to a confirmation of Pauling's theory that vitamin C improves immunity to diseases, as explained in the last section.
Revision of collagen molecular structure.
It was found that the diffraction data from native collagen could be explained by the 7/2-helical model better than, or at least the same as, the prevailing 10/3-helicals model.
The chemistry and structure of collagen.
NMR and x-ray studies of collagen model peptides.
The main focus is to review and to address the current state of knowledge in the field of NMR and x-ray analysis of triple helical model peptides.
Structure Analysis of a Collagen Model Polypeptide, (Pro–Pro–Gly)10
A detailed conformation study of the polypeptide (Pro–Pro–Gly)10, synthesized as a collagen model, has been done using X-ray diffraction. Several structures having the observed helical parameters
Molecular structure of the collagen triple helix.


Structure of Polyglycine II
This paper uses X-ray diffraction theory to deduce the three-dimensional structure of polyglycene II, a synthetic polymer consisting of an array of polypeptide chains made up solely of the amino acid glycene.
Polypeptide chain configurations in crystalline proteins
A systematic survey has been made of chain models which conform to established bond lengths and angles, and which are held in a folded form by N—H—O bonds, indicating that a further intensive study of these proteins, and in particular of myoglobin which has promising features of simplicity, may lead to a determination of the chain structure.
Infra-red spectra and structure of fibrous proteins
  • E. J. Ambrose, A. Elliott
  • Physics
    Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
  • 1951
The spectra of silk suture, porcupine quill, elephant hair, swan quill, gelatine and rat-tail tendon have been observed with polarized infra-red radiation. The first four materials give spectra which