Sandbox324: Difference between revisions
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Additional evidence is provided by InteroPro which provided more information about the classification of the protein. As well, the BLAST search gave results of matching proteins and the specific functions of the proteins. All results again matched what was suggested by Sprite and Blast, further solidifying that 4DIU is an esterase with alpha/beta-hydrolase activity. | Additional evidence is provided by InteroPro which provided more information about the classification of the protein. As well, the BLAST search gave results of matching proteins and the specific functions of the proteins. All results again matched what was suggested by Sprite and Blast, further solidifying that 4DIU is an esterase with alpha/beta-hydrolase activity. | ||
[[Image:InterPro.jpg]] | [[Image:InterPro.jpg]] | ||
'''Figure 2: '''Interpro Scan results for 4DIU displaying proposed characterization | '''Figure 2: '''Interpro Scan results for 4DIU displaying proposed characterization | ||
[[Image:Blast.jpg]] | [[Image:Blast.jpg]] | ||
'''Figure 3: '''Blast search for protein sequences matching 4DIU | '''Figure 3: '''Blast search for protein sequences matching 4DIU | ||
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</ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref>Vázquez-Mayorga, E.; Díaz-Sánchez, Á.; Dagda, R.; Domínguez-Solís, C.; Dagda, R.; Coronado-Ramírez, C.; Martínez-Martínez, A. Novel Redox-Dependent Esterase Activity (EC 3.1.1.2) for DJ-1: Implications for Parkinson’s Disease. International Journal of Molecular Sciences 2016, 17 (8), 1346. https://doi.org/10.3390/ijms17081346. | </ref>. This allows for the activity of the enzyme to be tracked by measuring the increase in absorbance over time. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a determined optimal pH of 6. Enzyme activity was measured via a change in absorbance at 405nm over 80 minutes. The data collected was consistent with that of hydrolases in other studies.<ref>Vázquez-Mayorga, E.; Díaz-Sánchez, Á.; Dagda, R.; Domínguez-Solís, C.; Dagda, R.; Coronado-Ramírez, C.; Martínez-Martínez, A. Novel Redox-Dependent Esterase Activity (EC 3.1.1.2) for DJ-1: Implications for Parkinson’s Disease. International Journal of Molecular Sciences 2016, 17 (8), 1346. https://doi.org/10.3390/ijms17081346. | ||
</ref> | </ref> | ||
'''Figure 3: ''' Trial 1 of 4DIU enzymatic activity measured over time via change in absorbance at 405nm in pH 8 buffer | |||
'''Figure 4: ''' Trial 1 of 4DIU enzymatic activity measured over time via change in absorbance at 405nm in pH 6 buffer | |||
[[Image:Enzymeactivity.jpeg]] | [[Image:Enzymeactivity.jpeg]] | ||
'''Figure | |||
'''Figure 5: ''' Trial 2 of 4DIU enzymatic activity measured over time via change in absorbance at 405nm in pH 6 buffer | |||
== Structural highlights of 4DIU == | == Structural highlights of 4DIU == | ||
