Consider five proteins with the properties shown in the following table. Answer the questions belowabout these proteins and justify your answers.Protein Subunit mass (Da) | Native mass (Da)10,00040,000120,000A15,000C20,00020,00025,00075,000E30,00060,000a) Which protein would migrate the slowest in an SDS-PAGE? Justify your results.b) Which protein would migrate the fast in a Native-PAGE? Justify your results.

Protein is an organic nitrogenous macromolecule that is essential for the health of humans. In the…

Answered: Consider five proteins with the…

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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Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
How can I calculate the unknown protein please
detail how cation exchange chromatography works and what you would use to elute your target protein. What protein information would you need to facilitate this approach? Would you need to do any protein engineering to utilize cation exchange chromatography, justify your answer?
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
Figure 1 represents the amino acid sequence of a G-protein coupled receptor (GPCR) as determine by mass spectrometry. *Figure 1 is shown as in the added image. Figure 1: The amino acid sequence of a GPCR as determined by mass spectrometry. (a) Describe a spectroscopic technique that you can use to determine the structure of the GPCR apart from mass spectrometry. (b) What is the purpose of the sequence sequences “MDYKDDDA” and “HHHHHH” at the N- and C-termini respectively?
The OXA-M290 protein is next purified by size exclusion chromatography. To determine the best type of size exclusion resin to use, the size of OXA-M290 must first be determined. Earlier, you determined the amino acid sequence of OXA-M290 (MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASSAKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYDTKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP). Based on the amino acid sequence, what is the molecular weight of this protein? You can use the free ProtParam tool (https://web.expasy.org/protparam/) to calculate the molecular weights of proteins. Make sure to include units in your answer. Note: The amino acid sequence reported earlier does not include the His-tag that was added to OXA-M290 by the pET-28a vector. However, you do not need to consider the amino acids in the His-tag in your answer to this question. For Context ONLY: For…
a) In the article the authors reference the canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do the authors suggest that other intermolecular interactions must be important to fully understand folding processes? https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6995338/pdf/nihms-1067149.pdf
A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex
You've isolated a novel protein, but you believe what you actually have is a mixture of the unmodified and phosphorylated protein. Which of these methods would be best for helping you to determine if you do indeed have a mixture of phosphorylated and non-phosphorylated protein, while also establishing other vital characteristics of this novel protein? O 2D-PAGE O SDS-PAGE O Isoelectric focusing O Native-PAGE
What is Protein folding? Give at least 3 diseases that results from protein misfolding. Explain each. Can you give me a brief explanation about this question? Not less than 3 sentences.
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%

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