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Sandbox Reserved 1072

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''Mycobacterium Tuberculosis'' Catalase Peroxidase (''mt''CP) is a [http://en.wikipedia.org/wiki/Protein_dimer homodimer] with each monomer consisting of two [http://en.wikipedia.org/wiki/Protein_domain domains]. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer.
''Mycobacterium Tuberculosis'' Catalase Peroxidase (''mt''CP) is a [http://en.wikipedia.org/wiki/Protein_dimer homodimer] with each monomer consisting of two [http://en.wikipedia.org/wiki/Protein_domain domains]. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer.
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[[Image:NterminalLOOP.png|300 px|right|thumb|Interlocking Hook]]
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[[Image:NterminalLOOP.png|300 px|left|thumb|Interlocking Hook]]

Revision as of 13:21, 24 March 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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Structure

Image:StructureWHOLE.png
Structure

Mycobacterium Tuberculosis Catalase Peroxidase (mtCP) is a homodimer with each monomer consisting of two domains. The two monomers interact through an interlocking hook formed by the N-terminal domains that stabilizes the formation of the dimer.

Image:NterminalLOOP.png
Interlocking Hook
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