. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
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3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
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- 1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?6. Complete the table below. If the sample is expected to show no reaction for a particular test, write NO RXN. If the sample is expected to show a reaction, describe the ideal observation for a positive result. Molisch's Bial's Test Iodine Test Benedict's test Cellulose Formation of purple interphase Formation of Fructose purple interphase Mannose Galactose1. What Substances Give The Same Reaction As Sugar With Nylander’s Test And How Do You Remove It? 2. by what other method can reducing sugars be differentiated from each other and from glucose? 3. what substances interfere with the tests for fructose? for lactose?
- 1. What type of reaction occurred when the samples (enumerated) reacted with the Molisch reagent? Give the chemical equation for each.a. Glucoseb. Sucrosec. Fructosed. Lactosee. Galactosef. Ribose 2. Explain the mechanism behind the test in simple terms. 3. What are the important products of the reaction of each sample?5. The proteins listed below are separated by (1) isoelectric focusing (IEF) followed by (2) sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE). A single sample of the protein mixture is placed at the top center of the gel to begin step 1. ID 1 2 3 4 5 6 7 8 Protein Collagen y-Globulin Insulin Fibronectin Lysozyme Pepsin Serum Albumin Myoglobin Molecular Weight 300,000 150,000 5,700 220,000 14,300 34,500 66,500 16,700 Conc pl 0.5 mg/L 4.7 1 mg/L 7.2 12 mg/L 5.3 5.8 11.0 5 mg/L 2 mg/L 10 mg/L - added prior to running IEF? left out of the process entirely? 4 mg/L 2 mg/L 1.0 4.9 7.1 A. Which of these proteins would electrophoresis NOT separate effectively? B. Which of these proteins would isoelectric focusing NOT separate effectively? Type fibrous a-helices globular protein globular protein fibrous protein enzyme digestive enzyme blood protein muscle protein C. Show the expected results after each step, by drawing qualitative diagrams similar to those shown in the class…1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.
- 14. A protein mixture consisting of proteins A, B, and C was subjected to various protein purification steps. First, the protein mixture was applied to an anion ion exchange column. When the column was washed with an increasing concentration gradient of chloride ions, the order of elution of the three proteins was B, then C, and finally A. Next, the protein mixture was chromatographed on a gel filtration column. The order of elution of the three proteins from this column was C, A, B. Finally, the protein mixture was passed over a chromatography column containing a Ni-NTA affinity matrix. Only protein A was retained by the column. Answer the following (i) Which protein (A, B, or C) has the highest and lowest positive charge (ii) Which protein has the highest and lowest mass (ii) Which protein has an affinity for the Ni-NTA matrix and why1. Identify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ? A. Hydrolysis B. Denaturation C. Heat denaturation D. Organic solvent denaturation E. Biuret test F. Hopkins – Cole Reaction G. Millon’s test H. Ninhydrin Test I. Sulfur test J. Xanthroproteic Test K. Chromatography L. Paper chromatography M. Competitive inhibition N. Noncompetitive inhibition O. Rancidity P. Hydrogenation 2. Identify what test is being described: Test that detects the free amino group in amino acids ? A. Hydrolysis B. Denaturation C. Heat denaturation D. Organic solvent denaturation E. Biuret test F. Hopkins – Cole Reaction G. Millon’s test H. Ninhydrin Test I. Sulfur test J. Xanthroproteic Test K. Chromatography L. Paper chromatography M. Competitive inhibition N. Noncompetitive inhibition O. Rancidity P. Hydrogenation 3. Identify what test is being described: A foreign substance, which is structurally similar to the substrate, competes for…1. Which of the following statement/s is/are TRUE for the protein sample?* The sample will give a positive result to Biuret test. All of A, B and C The sample will give a positive result to Ninhydrin test. The sample will give a positive result to Xanthoproteic test. 2. Extremely high pH causes folding of the protein molecules. * The statement is CORRECT. The statement is INCORRECT. 3.Negative with Biuret Test but positive with Ninhydrin Test, Xanthoproteic Test and Millon’s Test Glycine Tryptophan Tyrosine Methionine Albumin
- 5. In this investigation, you preformed qualitative tests for the presence of certain biochemical substances. How are the relative quantities of these biochemical substances determined? Use the internet or other sources to learn more about quantitative testing methods. Discuss two of them. (macromolecules lab questions) ( tests for presence of starch, sugar, proteins and fats)Consider the following properties of the protein components of a sample mixture as provided in the table below. Protein Molecular IpH Percentage of polar amino acid residues Weight (kDa) (%) АСЕ 200 7 20 CLU 25 65 DIA 100 10 40 НЕА 50 80a. Why is it important to eat food containing antioxidants? Write at leasttwo reactions to prove the answer. b. Write in four ways the following nucleotide sequence: ATGCA. c. Explain i. Hoogsteen pairing & ii. Hyperchromic effectiii. Epimers Iv. Mutarotaton v. Aldose vi. Anomers vii. Mutarotation