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| Attached Files |
| Name |
Description |
MIMEType |
Size |
Downloads |
EPSCoRprst.pdf
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EPSCoRprst.pdf |
application/pdf |
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0 |
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| Title |
Ancestral Sequence Reconstruction and Homology Modeling of Deoxyribonucleoside Kinase (dNK)
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| Type of Resource |
still image
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| Date Created |
2008-04-06
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| Digital Origin |
born digital
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| Rights Statement |
http://digital.uwyo.edu/copyright.htm
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| Keyword (topic) |
TBD
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| Series Title |
Undergrauate Research Day 2008
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| Creator(s) |
Thompson, Chandra
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| Genre |
Powerpoint/Pdf
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| Publisher |
University of Wyoming
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| Place of publication |
Laramie, Wyoming
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| Language |
eng
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| Summary |
Gene duplications are important in the evolution of genes and genomes because with gene duplication, proteins can evolve new functions. The dNK enzyme catalyzes the phosphorylation of dNs to dNMPs in the salvage pathway of deoxyribonucleosides essential for obtaining DNA precursors. Chordates have four forms of the enzyme TK2, dCK, and dGK specific for certain substrates. Arthropods have only one form of the enzyme dNK that can bind and phosphorylate all substrates. Based on phylogenetic analysis it appears that the dNK ancestor of chordates and arthropods is more similar to TK2-like enzymes than dNK. The hypothesis is that the dNK ancestor had greater substrate specificity and through neofunctionalization coupled to gene loss events dNK evolved broader specificity along the insect lineage. Ancestral sequences for dNK were created using ideal topologies from the Ecdysozoa and Coelomata hypotheses of species relationships. The sequences were then modeled to give a 3D structure. The energies for binding sites and the overall enzyme were analyzed for each hypothesis and other dNKs. The analysis of these energies indicates that Ecdysozoa is a more thermodynamically stable model, more likely phylogenetically, and that Coelomata and Ecdysozoa may have binding specificity that is more similar to TK2 than dNK.
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| Notes |
From - Undergraduate Research Day 2008 - Celebration of Research - Abstracts
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