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JMS/Sandbox/SMART HLA
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | <scene name='70/705122/ | + | <scene name='70/705122/Myoglobin_pairs/1'>aligned sperm whale w, pig p, grey seal s, and cat c. |
| - | + | w and p are a group, and s and c, are a group.</scene> | |
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/2'>general disk like structure of myoglobin, with heme ligand.</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/3'>hydrophobic residues (gly, ala,val,leu,ile,pro,phe,met,trp), that are on surface</scene> | ||
| + | <br/><br/><scene name='70/705122/Hydrophobic_core/1'>hydrophic residues only in the core</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/4'>hydrophic residues only in the core</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/5'>general statement that w and p differ in several amino acids</scene> | ||
| + | <br/><br/><scene name='70/705122/Sickle_hemoglobin_chain_close/1'>hemoglobin as classic case of hydrophobic patch based aggregation</scene> | ||
| + | <br/><br/><scene name='70/705122/Sickle_hemoglobin_chain_close/2'>zoomed out. hemoglobin as classic case of hydrophobic patch based aggregation</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/6'>divergent charged aa leading to delta 4</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/7'>stick/wireframe. divergent charged aa leading to delta 4</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/8'>mutations not in site of heme, so not o-binding. rather, net charge change leading to solubility increase.</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/9'>no negative to hydrophobic mutations for pig to whale, which would have increased net charge at the expense of creating hydrophobic patches.</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/10'>with halos. no negative to hydrophobic mutations for pig to whale, which would have increased net charge at the expense of creating hydrophobic patches.</scene> | ||
| + | <br/><br/><scene name='70/705122/Sickle_hemoglobin_chain_close/2'>zoomed out. hemoglobin as classic case of hydrophobic patch based aggregation</scene> | ||
| + | <br/><br/><scene name='70/705122/Myoglobin_pairs/11'>mutations overwhelming occur on the surface.</scene> | ||
</StructureSection> | </StructureSection> | ||
| + | |||
| + | all switches: 1,4,12,15,27,28,35,51,53,66,74,87,101,123,126,128,132,140,142,151 | ||
| + | charge switches: 12,53,87,113,116 | ||
| + | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:02, 23 June 2015
Your Heading Here (maybe something like 'Structure')
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all switches: 1,4,12,15,27,28,35,51,53,66,74,87,101,123,126,128,132,140,142,151 charge switches: 12,53,87,113,116
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
