Quiz 4 Question Pool Fall 2023

1. What is similar and what is different between the following chromatographic methods: Size Exclusion Chromatography; lon Exchange Chromatography; and Affinity Chromatography? This question requires you to compare, rather than simply describe the specified techniques. 2. What is similar and what is different between 1D (one-dimensional) and 2D (two-dimensional) protein gel electrophoresis? This question requires you to compare, rather than simply describe the specified techniques.

please solve this step by step calculations

Hi, hope you're doing great! I need help with a question, I have screenshot  thank you!

1. In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored?  2. How does SDS-PAGE separate proteins and peptides from each other? Explain. 3. Explain the Donnan Membrane Phenomenon. Why is it important for the homeostasis of the cell?

d/e/1FAIpQLSfTle9UfP15_VUqFI-ACEQd1XBykXv5Lr4dEMQbLJ1d6fCupw/viewform Students subjected three samples of five different molecules to gel electrophoresis as shown in Figure 1 A B C DE +2 3 Wells 4 8. Which of the following statements best explains the pattern seen on the * gel with regard to the size and charge of molecules A and B? 1 point molecules A and B are positively charged, and molecule A is smaller than molecule B. molecules A and B are positively charged, and molecule A is larger than molecule B. molecules A and B are negatively charged, and molecule A is smaller than molecule B. molecules A and B are negatively charged, and molecule A is larger than molecule B. Sign out

9 and 10 please

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

When the gel is removed from the chamber in SDS-PAGE, only the “pre-stained” protein standard is visible. There are no other proteins visible on the rest of the gel. Did something go wrong here? Why can’t you see the other proteins?

WELL NUMBER ORGANISM 1 2 3 4 6 7 8 Human +++ +++ + tt t++ + ++ Cow Chimpanzee t t+ Frog Monkey オt+ ャ+ ++ KEY: +++ Heavy Agglutination (Gel Solidification) + Medium Agglutination (Thick Liquid) Slight Agglutination (Flecks) No Reaction Lab Questions: 1. Animals that are most closely related to humans exhibited ichimpanzee agglutination. Heavy Medium Slight No 2. Animals that show little relation to humans exhibited cow agglutination. Heavy Medium Slight No 3. Which animal is most closely related to humans? Cow Chimpanzee Frog Monkey 4. Which animal is most unrelated to humans? Cow Chimpanzee (Frog Monkey

Do question 3

D Question 9 An enzyme assay of 2 mL of extract shows 7.3 U/mL and a biuret assay shows 4 mg/mL protein on the initial sample. It is salted out and the pellet is washed and resuspended in 0.4 mL buffer. It is re-assayed and shows 12.1 U/mL activity and 1.3 mg/mL protein. What is the change in fold purity for this sample? (answer to 2 decimal places)

Can you please help me to complete step by step the Log molecular weight I will appreciate your help

Justify all answers (show all work). 1. Minor changes in primary structure can have pronounced effects on biological function. Tetrameric hemoglobin, a₂³₂, dissociates into pairs of dimers aß to different extents depending on the protein primary structure. The standard Gibb energies of dissociation of normal adult hemoglobin A and of several mutants have been determined and are listed in the table below. Substitution in mutant Hemoglobin A, normal Richmond Kansas Georgia 102B; Asn → Thr 102B; Asn → Thr 95x; Pro → Leu AG® of dissociation (kcal/mole Hb) 8.2 6.0 65 5.1 3.6 (a) Write an equilibrium expression for the dissociation of hemoglobin tetramer into dimers. (b) For normal hemoglobin and its three mutants (variations) calculate the equilibrium constant for their dissociation from a tetramer into dimers. (c) How do the equilibrium constants for the dissociation of the hemoglobin mutants compare to that of normal hemoglobin?

Wh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…

Biochemistry Question Two - Explain how gel filtration chromatography (size exclusion chromatography) separates molecules on the basis of their mass/size.

Ethanol or Lactic acid G3P Руruvat Glucose G3P Руruvat Acetyl-CoA Citric Acid Охaloacetate

Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?

16. Your Excel data graph for Serial Dilution lab:** 16a. Include a clear and labeled graph of DF (x axis) versus Absorbance (y axis). See box above for expectations and review video tutorial of this Excel work. Do not graph two of your data points: your blank or your Cuvette #1 (DF=1). 1 Q A Multiple Styles W S X 3 E D $ 4 To C R F % 5 I T V U ^ 6 G Y 7 H U 8 J BN S ( 9 K M X

Standard curves You are setting up a standard curve for lysozyme. You have a stock vial containing 2 mg/ml of lysozyme and you have 2 ml in the vial. You will want to have a minimum of 1 ml of each concentration for the spectrophotometer. How would you proceed? (Saline is added to make the various concentrations). Concentration Am't stock lysozyme or am't of a previous dilution (note which) Amount saline Total volume wanted 1.00 mg/ml 0.75 mg/ml 0.50 mg/ml 0.375 mg/ml

*Answer only question 2. Prelude is in Question 1. 1. Briefly explain the principle behind the following techniques:(a) ion-exchange chromatography (b) gel filtration chromatography (c) affinity chromatography 2. Use three diagrams to illustrate the separation of three different proteins by these methods.

***not graded, just a practice problem I do not understand. Thank you so much!

Please don't provide handwriting solution

Exercise 1 Summarize the data below obtained from the protein experiments for determination of protein concentration in the form of a graph. Plot a graph containing a title and labels for both of the axis. Three readings were taken for each protein concentration. Find the averages and standard deviations for each reading and plot your graph using Microsoft EXCEL, complete with the error bars. This graph represents will be used to measure the protein concentration in an unknown protein solution. calibration curve for a protein assay (next experiment) where this Concentration of protein (Hg/mL) Absorbance, 595 nm 1 2 3 0.04 0.05 0.03 2 0.12 0.11 0.14 5 0.26 0.25 0.25 10 0.49 0.49 0.51 25 0.82 0.85 0.83 50 1.28 1.24 1.25

*the pictures are a guide for the answers* Part 3: Follow-up Questions 1. What is the type of bond formed between the two orange R groups?2. What is the type of bond formed between the two yellow R groups?3. Using the amino acid table on pg. 53 what is the only possible amino acid that can be represented by the orange tape?4. What possible interactions are occurring between the red R groups and the aqueous environment of the cytoplasm?