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- Explain the advantage of using Fluorescence Recovery After Photobleaching (FRAP) in determining protein localisation I notes = Notes Comments MAY 7.2. . questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. Calculate the overall charge (pH 7) on the following three polypeptides and answer the (A) Ser-Tyr-Ser-Met-Glu–His–Phe–Arg-Trp-Gly-Lys-Pro–Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu--Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His–Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu–Phe-Cys-Ser-Tyr-Ser-Met–Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (g) Which of the three peptides would migrate the furthest away from the anode in isoelectric fo- cusing (h) Which of the peptides would migrate the closest to the cathode in isoelectric focusing?…Structures: Purine Pyrimidine
- VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations. /u ivercarbUIT sugar, a phosphate group, and à nitrogenous base. 35.Most antimicrobial drugs currently in clinical use offer a great variety of unique targets for selective toxicity. Macrolides are broad-spectrum, bacteriostatic drugs that block elongation of proteins by inhibiting peptide bond formation between specific combinations of amino acids. Azithromycin is a broader spectrum antibiotic that is able disrupt INITIAL peptide bond formation. Which of the following protein structures will be altered, FIRST, by Azithromycin? a. the quaternary structure will be disrupted b. the secondary structure will be disrupted c. the tertiary structure will be disrupted d. the primary structure will be disrupted e. no levels of protein structure will be disruptedYou are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?
- Cells in the human liver contain glycogen, a polysaccharide that is used as a source of energy. This is a model of a typical glycogen granule: 42 22 AWARD Edit View Insert Format Tools Table be *** www 27544 Hals De w Jay MASCH Abh P CON p bo H S ******** 124 3. P WH ** patink The G k page flees P ******* 44651 CAPE Porn Tele de to MATE www 74 H Supe This type of granule may contain up to 30,000 (3 x 104) glucose subunits, making up the glycogen chains. A. How many ATP's could theoretically be produced when a granule of glycogen is hydrolyzed to glucose subunits that then enter glycolysis and respiration? B. Glycogen metabolism is regulated by insulin and glucagon. Both of these hormones are produced by the pancreas and act as signals that interact with a transmembrane receptor on target cells. Intracellular events involve protein kinase A that activates or inactivates enzymes involved in glycogen synthesis or degradation. Briefly describe what protein kinase A does to these proteins.Identify the biomolecule represented by the following image. O=P-O. 5' Base ОН 4" 1' 3 2' ОНThe octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.
- 10-20. Find the pH and the concentration of each species of lysine in a solution of 0.010 0 M lysine ·HCI, lysine monohydrochloride. The notation "lysine ·HCl" refers to a neutral lysine molecule that has taken on one extra proton by addition of one mole of HCl. A more meaningful notation shows the salt (lysineH†)(Cl ) formed in the reaction.a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? ExplainThe cationic polymerization of a-methylstyrene can be initiated by the BCI3/H2O initiating system. Assume the termination reaction occurs only by chain transfer to monomer by b-proton transfer. Draw the complete chemical structure for a poly(a-methylstyrene) containing three a-methylstyrene repeat units that results from this polymerization. 05 10:06 AM