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From Proteopedia
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- 17:42, 15 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14 (top)
- 17:36, 15 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:14, 15 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:12, 15 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:09, 15 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 19:34, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 19:32, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 19:31, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 19:22, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 19:18, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 18:52, 10 March 2024 (hist) (diff) Image:July22Exp2.png (July 12th, 2022, enzymatic assay data for five 200 𝜇𝐿 samples of varying 2O14 enzyme concentration plotted as absorbance versus time of reaction. The assay measured the hydrolysis reaction in samples containing uniform PNPA concentrations with varyi) (top)
- 18:51, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 18:49, 10 March 2024 (hist) (diff) Image:MMdata3.png (The plot of approximated velocity versus substrate volume for trial data from the Experiment of December 1st, 2022. The trial used eight 200 𝜇𝐿 samples containing 0.000625 mg/mL of 2O14 with PBS buffer, 7.0 pH and 2.0 𝜇𝐿, 6.0 𝜇𝐿, 8.0 ) (top)
- 18:49, 10 March 2024 (hist) (diff) Image:MMdata2.png (The plot of approximated velocity versus substrate volume for trial data from the experiment of November 18th, 2022. The trial used eight 200 𝜇𝐿 samples containing 0.000625 mg/mL of 2O14 with PBS buffer, 7.0 pH and 2.0 𝜇𝐿, 6.0 𝜇𝐿, 10.0 ) (top)
- 18:48, 10 March 2024 (hist) (diff) Image:MMeq.png (The Michaelis-Menten Equation.) (top)
- 18:47, 10 March 2024 (hist) (diff) Image:July22Exp1.png (Data for the 200 𝜇𝐿 Assay Samples Used for Assay Experiment Conducted on July 12th, 2022.) (top)
- 18:45, 10 March 2024 (hist) (diff) Image:MMdata1.png (The plot of approximated velocity versus substrate volume for trial data from the experiment of November 18th, 2022. The trial used eight 200 𝜇𝐿 samples containing 0.000625 mg/mL of 2O14 with PBS buffer, 7.0 pH and 2.0 𝜇𝐿, 6.0 𝜇𝐿, 10.0) (top)
- 18:42, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 18:33, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 18:01, 10 March 2024 (hist) (diff) Image:Bradforddialyzedmeasurements.png (Data of the Absorbance Measurements for Dilutions of the Purified, Dialyzed 2O14 Sample.) (top)
- 17:59, 10 March 2024 (hist) (diff) Image:PNPAreaction.png (Hydrolysis reaction of p-nitrophenyl acetate (PNPA).) (top)
- 17:58, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:51, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:46, 10 March 2024 (hist) (diff) Image:Bradfordplot.png (Microsoft Excel plot of absorbance versus concentration of six BSA standards from Bradford assay. The linear regression was adjusted from a larger data set to provide an appropriate slope intercept equation. The slope intercept equation was calculated b) (top)
- 17:45, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 17:00, 10 March 2024 (hist) (diff) Image:SDSPAGE.png (SDS-PAGE analysis of fractions eluted from Ni-NTA agarose column for 2O14 purification. The gel was stained with Coomasie blue. Elution 1, 2, 3, 4, and 5 are the fractions that were expected to contain the 2O14 protein. According to the standard, these ) (top)
- 17:00, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:51, 10 March 2024 (hist) (diff) Image:Growthplate.png (2O14 transformation plate growths. The transformation plate was made with LB medium, agar, and contained with 100 𝜇𝑔/𝑚𝐿 ampicillin.) (top)
- 16:41, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:36, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:35, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:31, 10 March 2024 (hist) (diff) Image:Insilicosum2.png (Image created in PyMOL molecular viewing software showing the structure of 2o14 with its five residues SER 171, ASP 339, HIS 342, GLY 209, and ASN 241 that belong to the proposed active site colored in yellow.) (top)
- 16:27, 10 March 2024 (hist) (diff) Image:Insilicosum1.png (Summary of most significant computational results for query 2O14 used to form hypothesis about 2O14's function.) (top)
- 16:26, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:19, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:11, 10 March 2024 (hist) (diff) Image:MCSA7.png (Hydrolysis of the 2-acetyl-1-alkyl-sn-glycero-3-phosphocoholine substrate from the reaction catalyzed by 1bwp. The bond circled in green is the ester bond that is cleaved. Image was created using Microsoft Paint and ChemDraw.) (top)
- 16:11, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:09, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 16:06, 10 March 2024 (hist) (diff) Image:MCSA6.png (Enzyme reaction catalyzed by 1j00, EC 3.1.1.5, lysophospholipase. The scheme was adapted from M-CSA and created in ChemDraw) (top)
- 16:06, 10 March 2024 (hist) (diff) Image:MCSA5.png (Enzyme reaction catalyzed by 1pp4, EC 3.1.1.86, rhamnogalacturonan acetylesterase. The scheme was adapted from M-CSA and created in ChemDraw.) (top)
- 16:05, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 15:59, 10 March 2024 (hist) (diff) Image:MCSA4.png (Enzyme reaction catalyzed by 1bwp, EC 3.1.1.47, 1-alkyl-2-acetylglycerophosphocholine esterase. The scheme was adapted from M-CSA and created in ChemDraw <ref name="Chemdraw"> Revvity Signals Software. ChemDraw | Revvity Signals Software. https://revvity) (top)
- 13:20, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 13:15, 10 March 2024 (hist) (diff) Image:MCSA3.png (M-CSA mechanism description information for 1avf and 1bbs, EC 3.4.23, aspartic peptidase) (top)
- 13:14, 10 March 2024 (hist) (diff) Image:MCSA2.png (M-CSA mechanism description information for 1bwp, EC 3.1.1.47, 1-alkyl-2-acetylglycerophosphocholine esterase <ref name="MCSA"> . Ribeiro, A. J. M.; Holliday, G. L.; Furnham, N.; Tyzack, J. D.; Ferris, K.; Thornton, J. M. Mechanism and Catalytic Site Atla) (top)
- 13:13, 10 March 2024 (hist) (diff) Image:MCSA1.png (Table 3. EC numbers of the six most significant SPRITE result enzymes with definitions from M-CSA) (top)
- 13:10, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 12:55, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 12:54, 10 March 2024 (hist) (diff) Studio:BASIL2023SUNYOswego2O14
- 12:50, 10 March 2024 (hist) (diff) Image:SPRITE4.png (SPRITE catalytic motif residue alignment image for a 1pp4 entry “1pp4_c00” and 2O14. 2O14’s residues are colored yellow. 1pp4’s residues are colored green. In the matches column 1pp4’s residues are listed first and 2O14’s residues are list) (top)
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