1. Most pure proteins are insoluble in pure distilled water but dissolve in dilute salt concentrations. However, the addition of high concentrations of neutral salts to an aqueous solution of protein causes it to precipitate. Name this phenomenon and suggest a molecular explanation for the observation that high concentrations of added salts decrease the solubility of proteins. 2. Capillary gel electrophoresis (CGE) forms part of a family of related techniques that comprise capillary electrophoresis (CE). Give a brief description of this technique with particular reference to its separation characteristics and applications.
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- 5. Consider two proteins with a pl of 4.5 and pl. of 7.7? Using a cation-exchange column, describe how these two proteins could be separated. Indicate which buffer you would prepare and how a salt gradient may be employed.5. What will happen to a protein if subjected to high tempuraturea?1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
- 1. Discuss how the pH and temperature affect the solubility of protein. 2. Explain "salting-in" in your own words.9. A patient with liver failure underwent a study of the electrophoretic spectrum of serum proteins. What physical chemical property of proteins underlies this method? A. Optical activity B. The ability to swell C. Hydrophilicity D. Inability to be purified by dialysis E. The presence of charge4. The table below describes a procedure in preparing standard solutions of a protein sample with different concentrations. (A) Determine the concentrations of each tube if the starting concentration of the protein is 500 mg ml (B) Determine the equation of the line if the concentration (x-axis) was plotted vs the absorbance (y-axis). (C) What is the concentration, in mg ml of the diluted unknown protein sample if the absorbance at 595 nm is 0.333? Tube Volume of protein, Volume of water, Final concentration, Absorbance mL mL mg ml [at 595 nm) 1 0.00 5.00 0.113 2 0.70 4.30 0.184 3 1.40 3.80 0.251 14 2.10 2.90 0.329 2.80 2.20 0.385 3.50 1.50 0.454 7 4.20 0.80 0.503 5.00 0.00 0.577
- 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?2. Vasopressin, a substance produced by the human body that regulates blood volume and pressure, is a nonapeptide with the following amino acid sequence. Describe the results you would expect when vasopressin is tested with the following reagents. sort GLY-ARG-PRO-CYS-ASN-GLN-PHE-TYR-CYS test xanthoproteic Millon's Hopkins-Cole nitroprusside observation A 250 25d ZYN CZ, ZINTEG DST ZW6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.
- 7. [10'] For a bacteriophage 77, the following data at zero concentration have been obtained: Sedimentation coefficient: $20,w = 453 S. Diffusion coefficient: D₂0. = 6.03×10-8 cm² s¹¹. 20,w Specific volume V20 = 0.639 cm³ g¹ Calculate the molecular mass M of the bacteriophage.1. Shown below is the chromatogram for some amino acid standards and two unknowns. Each unknown consists of just a single amino acid. Answer the following questions based on this chromatogram. Solvent Frort Ala Ser Asp Are UrkX Unk Y a) Explain the trend in the distances travelled by the standard amino acids. b) Calculate the R¢values of the standard amino acids and the two unknowns. Show your computations. c) Based on your calculations, what are X and Y? d) Are you able to identify X unambiguously? How about Y? e) If you are unable to identify either one of the unknown amino acids, think of a method by which you can separate them from each other. Explain your answer.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 why