Sandbox Reserved 1069: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Geoffrey C. Hoops, Madison Walberry, Austin S. Moore, Jessica Klingensmith, Kyle Colston

@@ Line 49: / Line 49: @@
 [[Image:FRET.png|200px|left|thumb| Figure 7. Labeled Cysteine resides measured with FRET showed the distance of the CTD of each monomer to be 24.0Å when saturated with Zn<sup>2+</sup>. Decrease in the Cys-Cys distance is indicative that both CTDs of YiiP were brought closer together.]]
 In contrast the main purpose of conformation change in the CTD is to stabilize the YiiP dimer and to act as a Zn<sup>2+</sup> sensor.
-This is possible because of the flexible loop that links the TMD and the CTD. This loop harbors the <scene name='75/756372/Bestsaltbridgetransparent/1'>salt bridge</scene> which serves as a hinge that allows movement of the CTD. Using [https://en.wikipedia.org/wiki/F%C3%B6rster_resonance_energy_transfer FRET] to measure the distance between the CTD of each monomer fluorescence quenching was observed as the concentration Zn<sup>2+</sup> increased, which supports that idea that Zn<sup>2+</sup> induces a stabilizing conformation change in the CTD.<ref>PMID:19749753</ref> CTD of both monomers were measured to be closer together when saturated with Zn<sup>2+</sup>.
+Using [https://en.wikipedia.org/wiki/F%C3%B6rster_resonance_energy_transfer FRET] to measure the distance between the CTD of each monomer fluorescence quenching was observed as the concentration Zn<sup>2+</sup> increased, which supports that idea that Zn<sup>2+</sup> induces a stabilizing conformation change in the CTD.<ref>PMID:19749753</ref> CTD of both monomers were measured to be closer together when saturated with Zn<sup>2+</sup>.