Sandbox Reserved 1069: Difference between revisions

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===Interlocking Salt Bridge===

The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two protomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's ~~binding sites~~ via interactions with the environment.

The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two protomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.

Sandbox Reserved 1069: Difference between revisions

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Revision as of 21:23, 29 March 2017 view source Madison Walberry (talk \| contribs) 48 edits No edit summary ← Older edit		Revision as of 21:23, 29 March 2017 view source Austin S. Moore (talk \| contribs) 111 edits No edit summary Newer edit →
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	===Interlocking Salt Bridge===		===Interlocking Salt Bridge===
	The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two protomers together. [[Image:Saltbridge.png\|200px\|left\|thumb\|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's ~~binding sites~~ via interactions with the environment.		The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two protomers together. [[Image:Saltbridge.png\|200px\|left\|thumb\|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.