Collagen Structure: The Madras Triple Helix and the Current Scenario

@article{Bhattacharjee2005CollagenST,
  title={Collagen Structure: The Madras Triple Helix and the Current Scenario},
  author={Arnab Bhattacharjee and Manju Bansal},
  journal={IUBMB Life},
  year={2005},
  volume={57}
}
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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171 Citations
Highly Influential Citations
6
Background Citations
49
Methods Citations
3

171 Citations

Stability of the hydration layer of tropocollagen: A QM study
TLDR
These water binding places on the surface of the triple helix can provide explanation on how an almost liquid‐like hydration environment exists between the closely packed tropocollagens and thus contribute to the elasticity of collagen.
How stable is a collagen triple helix? An ab initio study on various collagen and β‐sheet forming sequences
TLDR
The present study proves that by using first principles methods for calculating stabilities of supramolecular complexes, such as collagen and β‐pleated sheets, one can obtain stability data in full agreement with experimental observations, which envisage the applicability of QM in molecular design.
Unravelling the Role of Hydroxyproline in Maintaining the Thermal Stability of the Collagen Triple Helix Structure Using Simulation.
TLDR
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
TLDR
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.
Review of computer-aided models for predicting collagen stability.
TLDR
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%.
A molecular dynamics analysis of ion pairs formed by lysine in collagen: Implication for collagen function and stability
Molecular dynamic simulation studies on the effect of one residue chain staggering on the structure and stability of heterotrimeric collagen-like peptides with interruption.
TLDR
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.
A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence.
  • J. Bella
  • Biology, Chemistry
    Journal of structural biology
  • 2010
Sequence position and side chain length dependence of charge pair interactions in collagen triple helices.
TLDR
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.
TLDR
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.
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References

SHOWING 1-10 OF 59 REFERENCES
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.
TLDR
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.
TLDR
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
TLDR
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.
TLDR
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.
TLDR
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.
Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure.
Amino acid propensities for the collagen triple-helix.
TLDR
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
TLDR
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.
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