All logs
From Proteopedia
Combined display of all available logs of Proteopedia. You can narrow down the view by selecting a log type, the user name, or the affected page.
View (previous 50) (next 50) (20 | 50 | 100 | 250 | 500)
- 15:03, 25 November 2014 Abbey Evans (Talk | contribs) uploaded "Image:Steps.jpg" (In this proposed mechanism, the hydroxyl group of the 3-phosphoshikimate attacks the Oxygen of phosphoenolpyruvate (PEP). Simultaneously the double bonded CH2 of PEP accepts a proton creating a single bonded methyl group. The tetrahedral intermediate form)
- 14:58, 25 November 2014 Abbey Evans (Talk | contribs) uploaded "Image:Steps.JPG" (In this proposed mechanism, the hydroxyl group of the 3-phosphoshikimate attacks the Oxygen of phosphoenolpyruvate (PEP). Simultaneously the double bonded CH2 of PEP accepts a proton creating a single bonded methyl group. The tetrahedral intermediate form)
- 03:00, 25 November 2014 Abbey Evans (Talk | contribs) uploaded a new version of "Image:Mechanism.JPG"
- 01:36, 20 November 2014 Abbey Evans (Talk | contribs) uploaded "Image:Proline ring.jpg"
- 01:31, 20 November 2014 Abbey Evans (Talk | contribs) uploaded "Image:Prolinering.png"
- 01:24, 20 November 2014 Abbey Evans (Talk | contribs) uploaded a new version of "Image:Proline ring.PNG" (The active site of the 3-phosphoshikimate-1-carboxyvynltransferase is highlighted in green.There is evidence that the proline ring in the center is critical to the binding of a substrate and catalysis in general. It is undetermined however, the extent of )
- 01:24, 20 November 2014 Abbey Evans (Talk | contribs) uploaded "Image:Proline ring.PNG" (The active site of the 3-phosphoshikimate-1-carboxyvynltransferase is highlighted in green.There is evidence that the proline ring in the center is critical to the binding of a substrate and catalysis in general. It is undetermined however, the extent of )