Question 6.The solubility of globular proteins, when dissolved in water, is influenced by the factors/conditions listedbelow. Describe how these conditions would affect the solubility of the protein:a. pH of the buffer is the same as the pl of the proteinb. the pH of the solution is 12c. the solution is heated to 100°Cd. the solution contains 0.01 M NaCIc. the solution contains 70% ammonium sulphatef. the protein is dissolved in a 75% cthanol solutiong. urea is added to the solutionh. What does urea do to the protein structure?i. mercapto-ethanol is added to the solution

Globular proteins are the folded proteins that consists of hydrophilic aminoacids on the surface and…

Answered: Question 6. The solubility of globular…

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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In the Bradford protein determination, the color of a dye changes from brown to blue when it binds to a protein. The intensity of blue color (measured by absorbance of light at a wavelength of 595nm) is proportional to protein concentration. Protein (ug) Absorbance at 595nm 0.00 0.466 9.36 0.676 18.72 0.883 28.08 1.086 37.44 1.280 Use Excel to determine the equation of the line in the format of y = mx + b. (I tried y=0.0218x+0.4706 and it was wrong) Using the calibration curve for the Bradford protein determination in the previous question, determine the number of micrograms of protein in an unknown if it gave an absorbance of 0.973. I tried 23.505 and it was wrong
A synthetic amino acid has an ionizable side change (-OH) with a pKa of 6.54. Determine the isoelectric point for the amino acid. The other pKa values are 2.87 and 9.14. A. 6.54 B.7.84 C.6.00 D.4.71
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
1. The pka of an acid is partly dependent on the environment of the acid. What will be the effect of the following environmental changes on the pKa of a glutamic side chain? - 1. 1.4. protein denaturation
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:
9.
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
can you help me with this question? the list at the bottom is for part a.
Can you please explain how to solve this problem?
The CMC of SDS is 8.2 mM at 25 °C. Please describe the biological membrane solubilization when [SDS] is below or above 8.2 mM in the solution.
A protein has a dissociation equilibrium constant equal to 4.0um. What is the concentration of free ligand when the fraction of bound sites is 0.7
4. A protein solution is prepared by dissolving 350 µg of protein in 200 µL of water. A 150 μL sample of this solution is diluted to a total volume of 4.5 mL. How many mg of protein will be in a 2 mL sample of the diluted protein solution? Space to show your workings:

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