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.

[[Image:InterPro.jpg]][[Image:Blast.jpg]]

SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The ~~isolated~~ protein ~~was introduced~~ to p-nitrophenyl acetate ~~in a buffer with a pH of 6. Enzyme activity was measured via a change in absorbance at 405nm.~~ PNP ~~is a substrate that~~ when hydrolyzed produces a colored product ~~which~~ will lead to the solution absorbing more at 405nm. <ref>https://doi.org/10.1186%2F1471-2180-12-27</ref>. The data collected was consistent with that of hydrolases in other studies.

SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The hydrolase activity of the protein needed to be tested with a substrate known to work with hydrolases. This substrate is p-nitrophenyl acetate PNP when hydrolyzed produces a yellow colored product. The yellow product will lead to the solution absorbing more at 405nm. <ref>https://doi.org/10.1186%2F1471-2180-12-27</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 70 minutes. The data collected was consistent with that of hydrolases in other studies.

[[Image:Enzymeactivity.jpeg]]

== Structural highlights ==

Sandbox324: Difference between revisions

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@@ Line 15: / Line 15: @@
 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:Blast.jpg]]
-SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured via a change in absorbance at 405nm. PNP is a substrate that when hydrolyzed produces a colored product which will lead to the solution absorbing more at 405nm. <ref>https://doi.org/10.1186%2F1471-2180-12-27</ref>. The data collected was consistent with that of hydrolases in other studies.
+SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The hydrolase activity of the protein needed to be tested with a substrate known to work with hydrolases. This substrate is p-nitrophenyl acetate PNP  when hydrolyzed produces a yellow colored product. The yellow product will lead to the solution absorbing more at 405nm. <ref>https://doi.org/10.1186%2F1471-2180-12-27</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 70 minutes. The data collected was consistent with that of hydrolases in other studies.
 [[Image:Enzymeactivity.jpeg]]
 == Structural highlights ==