Collagen Structure: The Madras Triple Helix and the Current Scenario

@article{Bhattacharjee2005CollagenST,
  title={Collagen Structure: The Madras Triple Helix and the Current Scenario},
  author={A. Bhattacharjee and M. 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… Expand
View on Wiley
nucleix.mbu.iisc.ernet.in
153 Citations
Highly Influential Citations
6
Background Citations
48
Methods Citations
3

153 Citations

Citation Type

Citation Type

Stability of the hydration layer of tropocollagen: A QM study
  • 16
How stable is a collagen triple helix? An ab initio study on various collagen and β‐sheet forming sequences
  • 21
Collagen structure: new tricks from a very old dog.
  • J. Bella
  • Chemistry, Medicine
  • The Biochemical journal
  • 2016
  • 97
Review of computer-aided models for predicting collagen stability.
  • 4
  • PDF
A molecular dynamics analysis of ion pairs formed by lysine in collagen: Implication for collagen function and stability
  • 8
Molecular dynamic simulation studies on the effect of one residue chain staggering on the structure and stability of heterotrimeric collagen-like peptides with interruption.
  • 8
A new method for describing the helical conformation of collagen: dependence of the triple helical twist on amino acid sequence.
  • J. Bella
  • Chemistry, Medicine
  • Journal of structural biology
  • 2010
  • 43
Sequence position and side chain length dependence of charge pair interactions in collagen triple helices.
  • 2
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.
  • 11
Structural hierarchy controls deformation behavior of collagen.
  • 22
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 59 REFERENCES
Stabilization of the collagen structure by hydroxyproline residues
  • 11
Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution.
  • 792
A hypothesis on the role of hydroxyproline in stabilizing collagen structure.
  • 166
Stabilization of the triple-helical structure of natural collagen by side-chain interactions.
  • 43
Studies on collagen
  • 12
Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair.
  • 162
The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence.
  • 166
  • Highly Influential
Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure.
  • 32
Amino acid propensities for the collagen triple-helix.
  • 267
Crystal structure of the collagen triple helix model [(Pro‐Pro‐Gly)10]3
  • 215
...
1
2
3
4
5
...