On the Molecular Structure of Collagen

@article{Traub1969OnTM,
  title={On the Molecular Structure of Collagen},
  author={Wolfie Traub and Ada E. Yonath and D. Segal},
  journal={Nature},
  year={1969},
  volume={221},
  pages={914-917}
}
Several polytripeptide and polyhexapeptide models of collagen have the same triple helical conformation with one NH…O interchain H bond per tripeptide. Collagen itself probably has this structure. 
Infrared spectroscopy of collagen and collagen‐like polypeptides
TLDR
Previous and new infrared spectroscopic studies on collagen are considered and the infrared spectra of a number of polymers with collagen‐like features are presented.
Some Stereochemical Implications of the Molecular Conformation of Collagen
TLDR
A space-filling model of collagen has been constructed and shows that leucyl and phenylalanyl residues can be easily accommodated at position X of the collagen tripeptide sequence Gly.X, but are severely constrained by steric hindrance at position Y.
The biosynthesis of collagen. 1.
Micro-Heterogeneity in the Biosynthesis of Collagen Detailed analyses of the structure of the polypeptide chains of collagen has revealed a "micro-heterogeneity" of the amino acid sequences. Sequen...
POLYPEPTIDE MODELS OF COLLAGEN. SYNTHESIS OF (PRO‐PRO‐β‐ALA)n
The sequential copolymer (Pro-Pro-β-Ala)n has been synthesized as a model for collagen. Preliminary studies indicate that the polymer may bear conformational resemblance to collagen.
Investigation of fibrous structures. I. Computations for collagen
TLDR
The structure of collagen is investigated by means of an energy minimization procedure and it is seen that the unit height and the unit twist can strongly deviate from 2.86 Å, 36° values.
Conformational properties of polypeptide models of collagen.
TLDR
It appears likely that non-bonding interactions of the imino residue with the residue on its C-terminal may play a significant role in stabilizing collagen-like conformations.
The Macromolecular Workbench and its application to the study of collagen
TLDR
The authors used the study of collagen to test the functionality of MMWB, a software platform designed to integrate a diverse set of software and computer hardware to meet the needs of scientist performing molecular modeling.
Intracellular Steps in the Biosynthesis of Collagen
TLDR
Collagen biosynthesis involves several unusual posttranslational modifications which occur after assembly of amino acids into the three polypeptide chains of the molecule and which are essential for some of its critical structural features.
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References

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The molecular structure of collagen.
Structure of Collagen
TLDR
It has been found that it is possible to build up a two-bonded structure (two hydrogen bonds for three residues) while retaining all contacts within permissible values, and the actual parameters of the minor helix of the collagen structure have been re-determined.
Interchain hydrogen bonds via bound water molecules in the collagen triple helix
TLDR
It appears that this type of two‐bonded structure, in which one NH ⃛ O bond is to a water molecule, can explain several observations on the stability and hydrogen exchange properties of collagen itself and related synthetic polypeptides.
Fundamental dimensions of polypeptide chains
  • R. Corey, L. Pauling
  • Materials Science
    Proceedings of the Royal Society of London. Series B - Biological Sciences
  • 1953
TLDR
Data from many sources—X-ray diffraction analyses of crystals of organic acids, amides, peptides and related compounds; polarized infra-red studies of crystals—together with fundamental concepts of structural chemistry, now provide a basis for satisfactory knowledge and understanding of the dimensions and configurations of the amide group.
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