Sketch the appearance after visualization of a protein mixture containing the seven proteins(ovalbumin, insulin, fibrinogen, y-globulin, collagen, hemoglobin, myoglobin when subjected to SDS-PAGE.
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- Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly w/ 2D gel electrophoresis?Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly w/ isoelectric focusing?Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Мyoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above when subjected to SDS-PAGE?
- Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above if isoelectric focusing is done?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).1.0 0.9 Z 0.8 15. A pharmaceutical company studied the binding of three different compounds, X, Y, and Z, to a particular protein of interest. For each compound, the fractional saturation (v) was determined as a function of concentration. The results are shown in the figure. Which of the three compounds has the strongest affinity for the protein? Explain. 0.7 X 0.6 > 0.5 0.4 0.3 0.2 0.1 0.0 Y 0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0 L(μM)
- Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly using SDS page?Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen Hemoglobin (monomer) 6.6 115 7.1 16 Myoglobin 7.0 16.7 From the given table, draw the appearance after visualization of a protein mixture containing the seven proteins in the table when subjected to SDS-PAGE.Marker Proteins Molecular Weight (daltons) Distance 132,000 66,000 43,000 14,400 Serum Albumin (Dimer) Serum Albumin (Monomer) 23mm 32mm Ovalbumin 39mm 60mm Lysozyme Unknown 1 26mm Unknown 2 58mm Rabbit serum (albumin) 33mm 1.On semilog paper (provided below) plot the distance migrated by each standard protein as a function of molecular weight. Determine the molecular weight of the unknown proteins and the major protein found in rabbit serum (albumin) from this calibration curve. ii) Interferon is a protein of 25,000 Dalton. How far would it have migrated, land it been included in this experiment? iii) The average amino acid residue in a protein has a molecular weight of 120 Daltons. Assuming that your unknowns are average, how many amino acid residues do they contain
- Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. A trimeric protein containing three chains, each with a molecular weight of 60,000 Da (60 kDa).Several calibration curves were created for a series of protein standards of known molecular mass using molecular exclusion columns with different pore sizes. Which pore size should be used to perform molecular exclusion chromatography of proteins with a molecular mass near 10,000? 10 µm 5 nm 10 nm 1 pm 100 µm 50 nm 100 nm log (molecular mass) 7- 5mm 5.0 6.0 100 m Lum 10 m 7.0 8.0 9.0 100 um Elution volume (ml) 10.0 11.0 12.0A 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