Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- 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.arrow_forwardHow could you make the zwitterion of aspartic acid more soluble in water?arrow_forward6. 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?arrow_forward
- 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 pagearrow_forwardProtein solubility in aqueous solutions is dependent on ionic strength of the solution. True O Falsearrow_forwardThe 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.arrow_forward
- 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.arrow_forwardBeta-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 450.000arrow_forwardWhat 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 3arrow_forward
- 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.arrow_forward6. 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.arrow_forwardUV-vis spectroscopy can be used to determine protein and nucleic acid concentrations, provided the user knows the molar extinction coefficient of the protein or nucleic acid. Rank the wavelength absorption for the amino acids below from shortest wavelength to longest in the UV region.arrow_forward
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