Who discovered the triple helical structure of collagen?
This year marks the 50th anniversary of the coiled-coil triple helical structure of collagen, first proposed by Ramachandran’s group from Madras.
Which has triple helix structure?
Generally, the identity of a triple helix depends on the type of helices that make it up. For example: a triple helix made of three strands of collagen protein is a collagen triple helix, and a triple helix made of three strands of DNA is a DNA triple helix.
Why is collagen a triple helix?
Collagen folded into a triple helix is known as tropocollagen. Collagen triple helices are often bundled into fibrils which themselves form larger fibres, as in tendon….Collagen helix.
| Collagen triple helix | |
|---|---|
| InterPro | IPR008160 |
| SCOP2 | 1a9a / SCOPe / SUPFAM |
What is the structural importance of glycine residues in collagen?
In collagen, glycine is required at every third position, because the assembly of the triple helix puts this residue at the interior (axis) of the helix, where there is no space for a larger side group than glycine’s single hydrogen atom. For the same reason, the rings of the Pro and Hyp must point outward.
Who discovered Ramachandran plot?
Gopalasamudram Narayanan Ramachandran
Gopalasamudram Narayanan Ramachandran, or G.N. Ramachandran, FRS (8 October 1922 – 7 April 2001) was an Indian physicist who was known for his work that led to his creation of the Ramachandran plot for understanding peptide structure. He was the first to propose a triple-helical model for the structure of collagen.
Who discovered alpha helix and beta sheet?
PNAS papers by Linus Pauling, Robert Corey, and Herman Branson in the spring of 1951 proposed the α-helix and the β-sheet, now known to form the backbones of tens of thousands of proteins.
What is a Tropocollagen?
Tropocollagen is the basic structural unit of collagen, with a triple helix of polypeptide chains of approximately 1000 amino acid residues each, measuring 3000 Å long by 15 Å wide.
Who discovered collagen?
Very few know that it wasn’t Linus Pauling or Francis Crick but an Indian scientist from Madras who first discovered the structure of collagen, a type of protein. This remarkable discovery was made by Gopalasamudram Narayana Ramachandran, or simply GNR, in India in the early 1950s. Here’s his fascinating story.
Why is collagen left handed?
Left handed helices are formed because of the high content of proline and hydroxyproline rings, with their geometrically constrained carboxyl and (secondary) amino groups along with abundance of glycine. The left handed helices are formed without any intrachain hydrogen bonding.
How does glycine affect protein structure?
Conclusions. Glycine and proline residues have a major influence on the kinetics of loop formation in proteins. Glycine accelerates loop formation by decreasing the activation energy, whereas trans prolyl bonds slow loop formation by increasing the barrier height.
What is a glycine residue?
The Gly residue is unique among the amino acids in that all side chains are hydrogen atoms. Its conformation has greater freedom so that it can provide flexibility for adjacent residues. Because of this, it is not surprising that Gly plays a special role in enzyme structure and function.