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- Assignment on KetohexosesConstruct the structure of the following enantiomers or mirror images:1. D and L Fructose2. D and L Allulose3. D and L Sorbose4. D and L TagatoseOnly do the following- synthesize a monoglyceride and diglycerides and attach them below. Make sure to identify which is which!Phosphorylation of phosphatidylinositol yieldsa) Phosphatidylinositol 4, 5-biphosphateb) Phosphatidylinositol 3, 5-biphosphatec) Phosphatidylinositol 3, 4-biphosphated) Phosphatidylinositol 5, 6-biphosphate
- True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.topic: ISOLATION AND CHARACTERIZATION OF CARBOHYDRATES 1. Erythrose is an aldoterose. Describe the result when it is subjected to each of the following tests:a. Molisch’s Testb. Barfoed’s Testc. Benedict’s Testd. Seliwanoff’s Test2. Illustrate the reaction and identify the principle involved in the Nelson test.The α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?
- Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). II. What is the net ATP yield for the complete oxidation of all the fatty acid residues of the simple TAG? (Note: glycerol backbone is not included)Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the aboveUnbranched homopolymer of N-acetyl glucosamine is : 1.Cellulose 2.Chitin 3.Curcumin 4.Concanavalin A
- Choice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).PRECIPITATION OF PROTEINS What are peptides? Do all proteins possess peptide bonds? Do all proteins respond to Biuret’s test? What is the difference between coagulation and denaturation? Why is egg white used as an antidote for lead and mercurial poisoning? Explain its mechanism of action. 4.Why is silver nitrate used in the cauterization of wound? Explain your answer.Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. do not coy from other answers here
