Sandbox 14
From Proteopedia
(Difference between revisions)
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The planar base is also sandwiched between | The planar base is also sandwiched between | ||
<scene name='Sandbox_14/1wsu-recognition2/2'>three amino acids</scene>in the protein, which form a tight hydrophobic pocket. This is best seen using a | <scene name='Sandbox_14/1wsu-recognition2/2'>three amino acids</scene>in the protein, which form a tight hydrophobic pocket. This is best seen using a | ||
| - | <scene name=' | + | <scene name='Sandbox_14/1wsu-recognition3/1'>spacefilling diagram.</scene> |
The overall shape of the hairpin is recognized by contacts with several | The overall shape of the hairpin is recognized by contacts with several | ||
| - | <scene name=' | + | <scene name='Sandbox_14/1wsu-recognition4/1'>arginine and lysine amino acids.</scene> |
In particular, notice the intimate contact formed by both the charged nitrogen and hydrophobic carbon chain of | In particular, notice the intimate contact formed by both the charged nitrogen and hydrophobic carbon chain of | ||
| - | <scene name=' | + | <scene name='Sandbox_14/1wsu-recognition5/1'>arginine 606.</scene> |
Revision as of 22:20, 15 July 2008
Molecular Recognition in SelB Elongation factor SelB uses several methods to recognize the selenocysteine insertion sequence found in messenger RNA. The insertion sequence forms a hairpin loop with an unstacked guanine base in the loop. This guanine forms The planar base is also sandwiched between in the protein, which form a tight hydrophobic pocket. This is best seen using a The overall shape of the hairpin is recognized by contacts with several In particular, notice the intimate contact formed by both the charged nitrogen and hydrophobic carbon chain of
