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Sandbox Reserved 1678
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | Alginate lyase is a dimer (contains two domains). Being in a dimer form allows the protein to adapt to the seawater salinity from which is originates. | + | Alginate lyase is a <scene name='87/873240/Dimer/2'>dimer</scene> (contains two domains). Being in a dimer form allows the protein to adapt to the seawater salinity from which is originates. |
Each domain of the protein is made of <scene name='87/873240/Alpha_helices_and_beta_sheets/1'>6 alpha helices and 15 beta sheets</scene>. The alpha helices are shown in yellow, and the beta sheets are shown in pink. | Each domain of the protein is made of <scene name='87/873240/Alpha_helices_and_beta_sheets/1'>6 alpha helices and 15 beta sheets</scene>. The alpha helices are shown in yellow, and the beta sheets are shown in pink. | ||
Revision as of 01:26, 16 April 2021
| This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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Alginate Lyase (AlyC3)
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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
