Lead acetate solution is an agents of denaturation. Explain in 10 sentences the effect of each on proteins.
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Lead acetate solution is an agents of denaturation. Explain in 10 sentences the effect of each on proteins.
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- You are conducting an assay for glucose, wherein the color change of DNS due to reduction by glucose indicates glucose concentration. The tube contains: Water DNS Glucose solution of unknown concentration Buffer Which components would be included in your blank? DNS = 2-hydroxy-3,5-dinitrobenzoic acid Water DNS Glucose solution of unknown concentration BufferA mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?
- A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?A purified protein fraction has a total sample volume of 450 µL. The sample has a corrected A280 of 0.244, and the blank corrected A280 was 0.077. (Both values were measured with a path length of 1.00 cm.) If 5.50 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).Make use of the table below in answering the questions asked: Amino acid pK₁ pK₂ pK, Isoleucine 2.32 9.76 Leucine 2.32 9.74 Lysine 2.16 9.06 10.54 Tyrosine 2.20 9.21 10.46 I 1. Make sure to answer in two decimal places. What is the pl of the tripeptide ILY? 2. At pH 9.00, at which electrode will the ILY tripeptide be moving to? A. Anode B. Cathode C. The tripeptide will not move to either electrodes Make sure to show a solution or explanation for the answer.
- The side chain of acetyl-L-lysine-OMe has a pKa=10.5 and its acid-dissociation reaction is shown below. see attachment for Question D.The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsAfter staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
- N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at pH 7 with 375 mM NaCl. A dialysis membrane tube holds a 2.0 mL sample of the protein solution. The sample tube floats in a beaker containing 1.00 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na+, Cl-, and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 2.0 mL protein sample after dialysis in 150 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaCl] after a single dialysis: [NaCl] after a double dialysis: mM mMThe fosfomycin disc (200/50) also contains glucose-6-phosphate (G-6-P). Which ONE of the following best describes why this is the case? Select one: A. G-6-P increases the solubility of fosfomycin B. G-6-P is used to promote active transport of fosfomycin into the bacterial cell C. G-6-P is used in the formulation to correct glucose deficiencies promoted by fosfomycin D. G-6-P stabilises fosfomycin from spontaneous hydrolysis in aqueous solution E. G-6-P is an inhibitor of FosA that inactivates fosfomycinWhat are the different chemical test for the biomolecule nucleic acid?
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