Collagen: Difference between revisions
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== Exploring the Structure == | == Exploring the Structure == | ||
<applet load='1cag' size=' | <applet load='1cag' size='400' frame='true' align='right' /> | ||
A special amino acid sequence makes the tight collagen <scene name='Collagen/1cag/5'>triple helix</scene> particularly stable. Every third amino acid is <scene name='Collagen/1cag/1'>a glycine</scene>, and many of the remaining amino acids are <scene name='Collagen/1cag/3'>proline</scene> or <scene name='Collagen/1cag/4'>hydroxyproline</scene>. 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 <scene name='Collagen/1cag/2'>alanine</scene> 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 <scene name='Collagen/1cag/5'>triple helix</scene> particularly stable. Every third amino acid is <scene name='Collagen/1cag/1'>a glycine</scene>, and many of the remaining amino acids are <scene name='Collagen/1cag/3'>proline</scene> or <scene name='Collagen/1cag/4'>hydroxyproline</scene>. 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 <scene name='Collagen/1cag/2'>alanine</scene> amino acid in the position normally occupied by glycine, showing that it crowds the neighboring chains. | ||
