Qualitative Analysis of Proteins 1. Fill out the table below by providing the necessary information indicated per column. 2. As you have virtually conducted these qualitative tests for proteins, what do you think could be the essential practical or real-life applications of these tests?
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Qualitative Analysis of Proteins
1. Fill out the table below by providing the necessary information indicated per column.
2. As you have virtually conducted these qualitative tests for proteins, what do you think could be the essential practical or real-life applications of these tests?
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- Draw the chemical reaction involved in each qualitative reactions of proteins. Ninhydrin test (ninhydrin solution) Xanthoproteic test (concentrated nitric acid) Millon’s test (Millon's reagent) Hopkins-Cole test (glyoxylic acid) Biuret test (Biuret solution)Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVEIdentify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ? Hydrolysis Denaturation Heat denaturation Organic solvent denaturation Biuret test Hopkins – Cole Reaction Millon’s test Ninhydrin Test Sulfur test Xanthroproteic Test Chromatography Paper chromatography Competitive inhibition Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: Test that detects the free amino group in amino acids ? Hydrolysis Denaturation Heat denaturation Organic solvent denaturation Biuret test Hopkins – Cole Reaction Millon’s test Ninhydrin Test Sulfur test Xanthroproteic Test Chromatography Paper chromatography Competitive inhibition Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: A foreign substance, which is structurally similar to the substrate, competes for the active site of an enzyme ? Hydrolysis Denaturation Heat denaturation Organic solvent…
- Results and Discussion: Folin's McCarthy Sullivan Test: Samples: proline, methionine, alanine Reagents: sodium hydroxide (5N), Glycine (1%) and 10% sodium nitroprusside solution, 6N HCl -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (5N), followed by addition of few drops of glycine (1%) and 10% sodium nitroprusside solution (HANDLE WITH CARE)and vortex. Place the test tube in a hot water bath, maintained at 40 C, for 15 minutes. Cool the test tube in ice cold water for 5 minutes and add 0.5 ml of 6N HCl. Vortex the contents and allow to stant fpr 15 minutes at room temperature.In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.Multiple choice Which compound will yield a positive result with Salkowski test? (Picture 1) A, B, C, D In the emulsification of fats, which species is water soluble? (Picture 2) A, B, C, D In the emulsification of fats, which species is hydrophobic? (Picture 2) A, B, C, D
- A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, and phosphatidylcholine was applied to a hydrophobic interaction chromatography column. The column was then washed with increasingly nonpolar solvents. IWhat order would the lipids be eluted from the column?Qualitative and Quantitative Tests for Amino Acids and ProteinsComplete the table: Test Reagents Positive Result Positive Indication Ninhydrin test Xanthoproteic acid test Millon's test Hopkins Cole test Pauly's diazo Test Lead sulphide test Histidine test Isatin test Folin’s McCarthy Sullivan Test Nitroprusside TestMillon-Nasse Test Mix 1 mL of the sample and 5 drops of Millon-Nasse reagent. Boil the content gently for 30 seconds. Cool in water. Add 2 drops of freshly prepared 1% NaNO2 and warm gently. Observe the color of the precipitate and/or the solution. Question 1. Will all amino acids and proteins give a positive reaction to this test?Question 2. What causes the color of the solution or precipitate?
- Please pick among these 4 Protein chromatography is typically column-based:— lon-exchange— Reverse-phase/Hydrophobic interaction— Gel-filtration— AffinitySeparation of Amino Acids by Thin Layer Chromatography Lab Questions 1. Describe in detail Thin layer chromatographic experiment. Example: the theory behind it, how youwould prepare the materials to spot on the plate with different mobile amino acids and unknown andhow TLC Plate is developed and the reasoning behind which solvent/ solvent mixture should be used,along how to correctly identify of the unknown. 2. Calculate the Rf value if a solute travelled 5 cm from the base spot and the solvent front is 10 cmfrom the origin? 3. In a TLC experiment using a 70:30 mixture of Petroleum ether and ethyl acetate, a student noted thedevelopment of spots in the origin, what can you suggest about this observation?Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073x