User:Joanne Lau/sandbox 2

(Difference between revisions)

Revision as of 04:18, 6 December 2010

Molecular Playground banner: ClpX protein ‘spring cleans’ the cell by sending specific proteins to the ‘dumpster’.

Intro

Central Pore of the Hexameric ClpX is Conserved Asymmetry Falls into two classes of subunits

Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.

Angle changes and height changes, pulling a protein through to unfold it

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

@@ Line 6: / Line 6: @@
-===Unusual Features of the Hexameric ClpX===
+===Unusual Structural Features of Hexameric ClpX===
+Central Pore of the Hexameric ClpX is Conserved
+Asymmetry
+Falls into two classes of subunits
-Asymmetry and Falls into two classes of subunits
-===ClpX as an ATPase===
+===How ClpX Recognizes Specific Proteins===
-Angle changes and height changes, pulling a protein through to unfold it
+Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.
-===Central Pore of the Hexameric ClpX is Conserved===
+===Hexameric ClpX Unfolds and Drives Proteins Through its Aperture===
-Central pore is critical, conserved.
+Angle changes and height changes, pulling a protein through to unfold it
-===How ClpX recognizes specific proteins===
-Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.
-===Interaction between ClpX and peptidase ClpP gives rise to Protein Degradation Machinery===
+===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'''