Collagen: Difference between revisions

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[[Image:MotM 1cag bonds.gif|right]]

[[Image:MotM 1bkv.gif|right]]

A special amino acid sequence makes the tight collagen triple helix particularly stable. Every third amino acid is a glycine, and many of the remaining amino acids are proline or hydroxyproline. A classic triple helix is shown here, and may be viewed in the [[1cag]]. Notice how the glycine forms a tiny elbow packed inside the helix, and notice how the proline and hydroxyproline smoothly bend the chain back around the helix. In this structure, the researchers placed a larger alanine amino acid in the position normally occupied by glycine, showing that it crowds the neighboring chains.

A special amino acid sequence makes the tight collagen triple helix particularly stable. Every third amino acid is <scene name='Collagen/1cag/1'>a glycine</scene>, and many of the remaining amino acids are proline or hydroxyproline. A classic triple helix is shown here, and may be viewed in the [[1cag]]. Notice how the glycine forms a tiny elbow packed inside the helix, and notice how the proline and hydroxyproline smoothly bend the chain back around the helix. In this structure, the researchers placed a larger alanine amino acid in the position normally occupied by glycine, showing that it crowds the neighboring chains.

This collagen helix is taken directly from human collagen, and may be viewed in the [[1bkv]]. Notice that the top half is very uniform, where the sequence is the ideal mixture of glycine and prolines. At the bottom, the helix is less regular, because many different amino acids are placed between the equally-spaced glycines.

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@@ Line 17: / Line 17: @@
 [[Image:MotM 1cag bonds.gif|right]]
 [[Image:MotM 1bkv.gif|right]]
-A special amino acid sequence makes the tight collagen triple helix particularly stable. Every third amino acid is a glycine, and many of the remaining amino acids are proline or hydroxyproline. A classic triple helix is shown here, and may be viewed in the [[1cag]]. Notice how the glycine forms a tiny elbow packed inside the helix, and notice how the proline and hydroxyproline smoothly bend the chain back around the helix. In this structure, the researchers placed a larger alanine amino acid in the position normally occupied by glycine, showing that it crowds the neighboring chains.
+A special amino acid sequence makes the tight collagen triple helix particularly stable. Every third amino acid is <scene name='Collagen/1cag/1'>a glycine</scene>, and many of the remaining amino acids are proline or hydroxyproline. A classic triple helix is shown here, and may be viewed in the [[1cag]]. Notice how the glycine forms a tiny elbow packed inside the helix, and notice how the proline and hydroxyproline smoothly bend the chain back around the helix. In this structure, the researchers placed a larger alanine amino acid in the position normally occupied by glycine, showing that it crowds the neighboring chains.
 This collagen helix is taken directly from human collagen, and may be viewed in the [[1bkv]]. Notice that the top half is very uniform, where the sequence is the ideal mixture of glycine and prolines. At the bottom, the helix is less regular, because many different amino acids are placed between the equally-spaced glycines.