Sandbox Reserved 1692
From Proteopedia
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Amino Acids <scene name='89/892735/Highlighting_amino_acids/2'>85, 150, 166, 170, 202, 220, 275, and 331</scene> provide important interactions for binding. | Amino Acids <scene name='89/892735/Highlighting_amino_acids/2'>85, 150, 166, 170, 202, 220, 275, and 331</scene> provide important interactions for binding. | ||
== Structural highlights == | == Structural highlights == | ||
- | + | Secondary Structure: In this protein, there are around 30 anti-parallel beta sheets, two small hydrophobic alpha helices, and one alpha helix. The anti-parallel beta sheets provide further stabilization, through strong hydrogen bonding in the backbone, of the protein compared to parallel beta sheets. The hydrophobic alpha helices provide structure for the formation of the active site. | |
== Other important features == | == Other important features == | ||
Revision as of 05:12, 8 November 2021
This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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Structure of FoRham1 (maybe something like 'Structure')
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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