User:Joanne Lau/sandbox 2
From Proteopedia
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
| - | Molecular Playground banner: ClpX ‘spring cleans’ by dumping some proteins and refolding others. More at | + | Molecular Playground banner: ClpX ‘spring cleans’ by dumping some proteins and refolding others. More at MolecularPlayground.org. |
Intro | Intro | ||
Revision as of 20:52, 9 December 2010
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Molecular Playground banner: ClpX ‘spring cleans’ by dumping some proteins and refolding others. More at MolecularPlayground.org.
Intro
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Contents |
Unusual Structural Features of Hexameric ClpX
Central Pore of the Hexameric ClpX is Conserved, Asymmetry, Falls into two classes of subunits
How ClpX Recognizes Specific Proteins
Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.
Hexameric ClpX Unfolds and Drives Proteins Through its Aperture
Angle changes and height changes, pulling a protein through to unfold it
Interaction between ClpX and ClpP results in a powerful Protein Degradation Machinery
Interaction between ClpX and ClpP donut in a row, which domain interacts. Critical to determine ClpX role as a chaperone or a protease. How powerful
References
