AC2GThis a photograph of an actual polyacrylamide gel that has been run with samples of protein. For eachquestion, write the letter from the item in the gel that best matches the word or concept that isdescribed. Answers may be used once, more than once, or not at all. There may be more than onecorrect answer per question.1. Band2. Lane3. Well4. Will protein migrate through the gel from A to B or will it migrate from B to A?5. Which end is nearest the negative electrode, A or B?6. Which contains smaller protein fragments, F or G?7. Which letter indicates the highest concentration of protein fragments that are the same size8. Where would a sample of protein be loaded?B.

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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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Give 2 structural features in each of the given proteins below that make them perform their biological roles effectively (structural features that directly make them effective in their respective biological roles). Explain how each structural feature directly contributes to proteins’ biological roles. hemoglobin immunoglobulin
When a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
How could you make the zwitterion of aspartic acid more soluble in water?
6. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of SDS the protein gives three bands with molecular m of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. a. Approximately how many amino acids are present in a 400 kDa protein. (show work) b. How many grams would there be in a nanomole of this protein? (show work) C. What is the purpose of adding DTT? d. How many subunits does the protein have, and what are their molecular weights?
2 Keratin is a type of found in the cytosol, which means its hydrophobic amino acids are Select one: b. O c. a. amino acid, skin, exposed on the surface of the protein protein, hair, exposed on the surface of the protein protein, liver, exposed on the surface of the protein protein, liver, not exposed on the surface of the protein e. protein, hair, not exposed on the surface of the protein O d. Lue Dec 8 at 5pm of humans. On a cellular level, keratin is found in the Jump to... 45 Next page
Protein solubility in aqueous solutions is dependent on ionic strength of the solution. True O False
The figure below shows the structures of the blood group antigens O, A and B.List all nucleotide sugars and glycosyltransferase enzymes that are needed to construct blood group antigen A.
Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.
Beta-tubulin has a molecular mass of 55 kDa, Approximately how many amino acids are found in Beta-tubulin? O 45 O 450 O 4,500 O 45.000 O 450.000
What is the correct pairing of the Ramachandran plots with the protein structures they quantify? A B с A-2, B-1, C-3 A-1, B-2, C-3 A-2, B-3, C-1 A-3, B-1, C-2 A-3, B-2, C-1 3
Draw a UV-Vis spectrum for each protein (shown in the table below) (A, B, C, and D) from 240 – 480 nm if they were all present at 20 µM.
6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.

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