4. The table below describes a procedure in preparing standard solutions of a protein sample withdifferent concentrations.(A) Determine the concentrations of each tube if the starting concentration of the protein is 500mg 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 theabsorbance at 595 nm is 0.333?TubeVolume of protein,Volume of water,Final concentration,AbsorbancemLmLmg ml[at 595 nm)10.005.000.11320.704.300.18431.403.800.251142.102.900.3292.802.200.3853.501.500.45474.200.800.5035.000.000.577

Proteins are chain of amino acids linked by the peptide bonds, a covalent bond. Its concentration…

Answered: 4. The table below describes a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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What are the components of the buffers used for protein hydrophobic column chromatography and explain how do they work?
Gradient PAGE uses differing gel concentrations along the length of the gel to achieve optimalseparation of proteins of a wide range of molecular weight proteins. How does the staining pattern of these types of gels differ from nongradient PAGE?
19. 150 mCi of D2O is injected in your patient. 10% of D2O is excreted. The concentration of D2O in a plasma sample is found to be 0.4 mCi/100 ml. What is your patient' s Total Body Water in L? 20. the diffusion coefficient states that: A. the larger the molecular radius of the solute, the slower the rate of diffusion B. the more viscous the solution, the slower the rate of diffusion C. the smaller the molecular radius of the solute, the faster the rate of diffusion D. the more viscous the solution, the faster the rate of diffusion E. the larger the molecular radius of the solute, the faster the rate of diffusion 21 You are experimenting on diffusion rates in lab. Down the center of Beaker A is a semipermeable membrane. On one side of the membrane in Beaker A is a 100mM solution of CaCl2; on the other side is pure water.Down the center of Beaker B is a semipermeable membrane. On one side of the membrane in Beaker B is a 10mM solution…
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
a) The pl of a protein is 9.0. What will be the net charge (positive, negative or neutral) on the protein under the following conditions: A buffer with pH 9.0: A buffer with pH 7.0: A buffer with pH 10.0: b) Your protein is present in a sample buffer which has a pH 7.0. The sample is applied to an ANION EXCHANGE column. Will protein 1 bind to the beads on the column? Yes/No
If you added three proteins (Protein A, pI 5.0; Protein B, pI 6.0; Protein C, pI 7.0) to an anion exchange column equilibrated with bicine buffer, pH 8.5, in what order would these protein be expected to elute as the column was loaded, washed, and then increasing amounts of NaCl were added?
(c) The figure below shows the measured osmotic pressure, II / c, against the mass concentration c of the polymer for polymer solutions A, B, C, and D. The temperature and solvent are constant. D П B A (i) Rank the polymers according to their molar mass. (ii) In which polymer solution is the quality of the solvent the poorest? What type of solvent is present in sample C? Explain your answer. (iii) Which polymers could have the same chemical composition Explain your answer.
47. Tretinoin gel (RETIN-A MICRO) is avail- able in two strengths: 0.1% w/w and 0.04% w/w. Which of these represents equivalent concentrations of the two strengths? (a) 15 mg/15 g and 30 mg/30 g (b) 5 mg/5 g and 0.06 g/15 g (c) 15 mg/15 g and 60 mg/15 g (d) 30 mg/30 g and 6 mg/15 g 47. (d) 30 mg/30 g and 6 mg/15 g
7. You want to separate these four proteins in a mixture: Isoelectric point Mol. Weight (kDa) Protein A 4.1 80 Protein B 9.0 81 Protein C 8.8 37 Protein D 3.9 172 Which of the following would be the best order in which to run chromatography columns? A) Anion-exchange at pH 3, then size exclusion B) Cation-exchange at pH 3, then size exclusion C) Cation-exchange at pH 3, then anion-exchange at pH 3 D) Anion-exchange at pH 3, then cation-exchange at pH 3 E) Size exclusion, then cation-exchange at pH 3 F) Size exclusion, then anion-exchange at pH 3
5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?
To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?
Which method of chromatography would be the most appropriate for separating mixtures of thefollowing peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA(b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE(c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5?Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–ValPeptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-IlePeptide 2: Arg–Ile–Pro–Lys–Cys–Met–Lys

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