Collagen Structure: The Madras Triple Helix and the Current Scenario

  title={Collagen Structure: The Madras Triple Helix and the Current Scenario},
  author={Arnab Bhattacharjee and Manju Bansal},
  journal={IUBMB Life},
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 protein secondary structures in that it requires a very specific tripeptide sequence repeat, with glycine being mandatory at every third position and readily accommodates the imino acids proline/hydroxyproline, at the other two positions. The original structure was postulated to be stabilized by two interchain… 
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This study constructed a collagen model with typical triple helix structure and calculated the hydrogen bond energy between collagen alpha chains and found that thermal unfolding did not occur simultaneously along the entire molecule, but started in the regions with less Hyp content.
Collagen structure: new tricks from a very old dog.
  • J. Bella
  • Chemistry, Biology
    The Biochemical journal
  • 2016
The current understanding of the structure of the collagen triple helical domain (COL×3) is summarized and an overview of some of the new developments in collagen molecular engineering aiming to produce novel collagen-based materials with superior properties are given.
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This study assembled data on a large number of collagen-like peptides to build the first Markov chain model for predicting the stability of the collagen at different temperatures, simply by analyzing the amino acid sequence, and validated the model with accuracy between 82% and 92%.
Molecular dynamic simulation studies on the effect of one residue chain staggering on the structure and stability of heterotrimeric collagen-like peptides with interruption.
This is the first report on the structural effect on the heterotrimeric models with G4G and G1G breaks present simultaneously in the constituent chains with difference in one residue chain staggering.
Sequence position and side chain length dependence of charge pair interactions in collagen triple helices.
The effect of salt on triple helix stability is examined and it is observed that increased salt concentration reduces the thermal stability of heterotrimers by an average of 5 °C, but does not disrupt helix assembly.
Orchestration of Structural, Stereoelectronic, and Hydrogen-Bonding Effects in Stabilizing Triplexes from Engineered Chimeric Collagen Peptides (Pro(X)-Pro(Y)-Gly)6 Incorporating 4(R/S)-Aminoproline.
A new class of collagen analogues-chimeric cationic collagens-wherein both X- and Y-sites in collagen triad are simultaneously substituted by a combination of 4(R/S)-(OH/NH2/NH3(+)/NHCHO)-prolyl units and triplex stabilities measured at different pHs and in EG:H2O are described.


Stabilization of the collagen structure by hydroxyproline residues
The molecular structure of collagen is now accepted to be based on a triple-stranded coiled-coil, in which the three strands are held together predominantly by hydrogen bonds. Recent experimental
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.
A hypothesis on the role of hydroxyproline in stabilizing collagen structure.
Stabilization of the triple-helical structure of natural collagen by side-chain interactions.
The study presented here is the first application of conformational energy computations to a real sequence in the collagen molecule and it is shown that side-chain-backbone interactions contribute substantially to the stabilization of the triple-helical structure of collagen with a natural sequence.
Studies on collagen
The proposed structure of collagen is in good agreement with the infra-red and X-ray data and also fits in broadly with the amino-acid composition and other properties of collagen.
Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair.
The EKG structure suggests a molecular mechanism for stabilization at neutral pH values, where both Glu and Lys are ionized, but suggest that this occurs because of the effects of ionization on the individual residues, rather than ion pair formation.
The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence.
The novel packing arrangement displayed by the T3-785 structure, compared with those of collagen-like peptides with more imino acid-rich sequences indicates the sequence dependence of intermolecular assemblies in collagen as well.
Amino acid propensities for the collagen triple-helix.
A complete scale of amino acid propensities for the collagen triple-helix conformation with its Gly-X-Y repeating sequence is determined for the first time, providing a first step in defining sequence-dependent variations in local triple- Helix stability and binding.
Crystal structure of the collagen triple helix model [(Pro‐Pro‐Gly)10]3
The first report of the full‐length structure of the collagen‐like polypeptide [(Pro‐Pro‐Gly)10]3 is given, which suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.