You have an aqueous solution of hemoglobin (pl = 6.8) at pH 6.5, and currently the proteins are soluble. If you had 1 M HCl and 1M NaOH at yourdisposal, what could you do to precipitate the albumin out of solution?O add NaOH to the solutionadd HCl to the solutionadd NaOH to the solution, then add equal volume of HCl to the solutionO add HCl to the solution, then add equal volume of NaOH to the solutionAn error has been detected in your answer. Check for typos,miscalculations etc. before submitting your answer.Submit AnswerTry Another Version1 item attempt remaining

pH affects the ionisation of amino acids and can thus influence the nature and distribution of…

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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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Oils can be converted to fats by a commercial process catalyzed bynickel which is called partial hydrogenation. In relatively mild conditions (180ºC and pressures of about 1.33 atm) a sufficient number of double bonds are hydrogenated and solidify liquid oils. This solid material, margarine, has a consistency similar to butter. Come up with a practical reason why oils don'tthey are completely hydrogenated during commercial hydrogenation processes.
Which of the following statements most closely describes the quaternary structure change of deoxyhemoglobin when it binds oxygen? Group of answer choices the hydrophobic core of each monomer undergoes significant repacking the two beta chains of the molecule get closer by about 7 Angstroms the two beta chains of the molecule get closer by about 7 nanometers one alpha/beta dimer of the tetramer rotates by 90 degrees with respect to the other a new set of noncovalent contacts forms between the two alpha subunits
27)
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.
You have a protein with MW 48kDa. How many grams of protein are in a 200 mL sample at 50 μM?
A mixture of two proteins (both with mass of 50 kDa) with an molecular isoelectric points of 7.8 and 8.9, respectively, is in a buffered solution at pH 7. Which type of liquid chromatography would be used to separate these two proteins? O a. O b. O C. d. e. anion exchange chromatography size-exclusion column gel filtration Ni-NTA column cation exchange chromatography
Consider a mixture comprised of the proteins attached: Protein that will most strongly bind to an anion exchange column? Protein that will elute first in gel filtration chromatography? Protein that will elute last in hydrophobic interaction chromatography? Protein that will elute last in carbohydrate containing column?
Proteins and Amino Acids A. Acid-base properties of proteins: 1. Data a. Color phenolphthalein-NaOH solution -before adding casein : colorless - after adding casein :colorless cloudy b. Color of methyl orange-HCl solution - before adding casein :Blue - after adding casein : Pink 2. Why did the solutions change color? 3. Which property of proteins is illustrated by the above? 4. Why as methyl orange used in place of phenolphthalein in the second part of this procedure? B. Isoelectric point of casein: 1. Data Initial pH of milk Final pH of milk 2. What is the isoelectric point of casein? C. Denaturation of proteins: A. pH 1. Observations: a. Tube no. 1: concentrated HCI b. Tube No. 2: concentrated HNO, c. Tube No. 2: concentrated H,SO, 2. Which structure(s) of the protein were disrupted in this procedure?
The kidneys function to eliminate ammonia from the blood. Based on ammonia’s pK value, what is the molecular form that predominates in the blood? Could this molecule easily diff use through the hydrophobic lipid membrane of a kidney cell? Explain.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
Three proteins with an overall charges of 0, -5, and -8 are passed through an anion exchange column equilibrated in a buffer with low ionic strength and eluted with an increasing gradient of salt in a buffer. Which protein will elute last from the column? 1. Protein with no charge. 2. Protein with eight negative charges. 3. Protein with five negative charges. 4. Both charged proteins will elute at the same time.
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…

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