Sandbox Reserved 325: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 13: | Line 13: | ||
==Structure== | ==Structure== | ||
<Structure load='2f6l' size='300' frame='true' align='left' caption=' | <Structure load='2f6l' size='300' frame='true' align='left' caption='Chorismate Mutase' scene='Sandbox_Reserved_325/Chainbows/1' /> | ||
Chorismate mutase is a homodimer which has an predominantly α-helical structure <ref name="pizza" />. There are 10 α-helices spread across the two monomers of chorismate mutase <ref name="pizza" />. Approximately 86% of the amino acid residues are in the α-helical formations <ref name="pizza" />. The α-helical structure of ''M. tuberculosis'' chorismate mustase similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli'' <ref name="pizza" />. It holds its dimeric state in a protein concentration as low as 5 nM <ref name="pizza" />. There are no β-sheets present in chorismate mutase <ref name="CMArt2" /> | Chorismate mutase is a homodimer which has an predominantly α-helical structure <ref name="pizza" />. There are 10 α-helices spread across the two monomers of chorismate mutase <ref name="pizza" />. Approximately 86% of the amino acid residues are in the α-helical formations <ref name="pizza" />. The α-helical structure of ''M. tuberculosis'' chorismate mustase similar to the chorismate mutases of ''S. cerevisae'' and ''E. coli'' <ref name="pizza" />. It holds its dimeric state in a protein concentration as low as 5 nM <ref name="pizza" />. There are no β-sheets present in chorismate mutase <ref name="CMArt2" /> | ||