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(Difference between revisions)
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====3His/1Cys Motif==== | ====3His/1Cys Motif==== | ||
== Mechanism of Action == | == Mechanism of Action == | ||
| - | <scene name='69/694239/Hydrophobicity_int_residues/ | + | <scene name='69/694239/Hydrophobicity_int_residues/3'>Hydrophobic residues</scene> on the alpha helices of the zinc binding domain participate in van der waals interactions that induce a conformational change in the protein when zinc binds. When Zinc binds, the <scene name='69/694239/Czbd_with_helices_labeled/2'>𝝰1 helix</scene> becomes straightened, burying nonpolar side-chain residues, influencing activity of DgcZ |
== Zinc Ligand(s) == | == Zinc Ligand(s) == | ||
Revision as of 02:53, 31 March 2017
| This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Diguanylate Cyclase DgcZ from Escherichia coli
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
