Sandbox Reserved 1691
From Proteopedia
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Threonine is Amphipathic, which means it has both hydrophilic and hydrophobic parts. Serine, Threonine, and Lysine are Polar. Polar hydrophilic amino acids are important in ligand binding to the substrate because it makes the binding site precisely positioned for hydrogen bonding to the hydroxy and carboxylate groups of the substrate. I found that the Inotisol rings on the end have a lot to do with binding.<scene name='89/892734/The_other_amino_acids_view_3/1'> The other Amino acids</scene> for binding are Thr 312, Lys 270, Ala 291, Asp 156. These key amino acids are important because they participate in hydrogen bonds, hydrophobic, and ionic bonds. | Threonine is Amphipathic, which means it has both hydrophilic and hydrophobic parts. Serine, Threonine, and Lysine are Polar. Polar hydrophilic amino acids are important in ligand binding to the substrate because it makes the binding site precisely positioned for hydrogen bonding to the hydroxy and carboxylate groups of the substrate. I found that the Inotisol rings on the end have a lot to do with binding.<scene name='89/892734/The_other_amino_acids_view_3/1'> The other Amino acids</scene> for binding are Thr 312, Lys 270, Ala 291, Asp 156. These key amino acids are important because they participate in hydrogen bonds, hydrophobic, and ionic bonds. | ||
- | Final | + | <scene name='89/892734/Final_view_of_the_active_site/2'>Final View</scene> of the active site with all the important amino acids |
<scene name='89/892734/Amino_acids_156-159/1'>Amino_acids 156-159</scene> are important part of drug binding site <ref>33172890 </ref>. | <scene name='89/892734/Amino_acids_156-159/1'>Amino_acids 156-159</scene> are important part of drug binding site <ref>33172890 </ref>. |
Revision as of 06:38, 7 December 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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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
- ↑ 33172890