Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen Y-globulin 5.8 340 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?
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A: Given values: Distance traveled by the dye front = 7 cm Distance traveled by the protein = 2.8 cm
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Q: Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 =…
A: pK refers to pH at which a particular group is exactly 50% ionized. A tripeptide is a peptide…
Q: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340…
A: The isoelectric point of a Protein: Isoelectric point is the pH at which a protein forms its…
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Q: How do you solve these? Please explain
A: Hey, since there are multiple questions posted, we will answer first question. If you want any…
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Q: Mr standards without with (kDa) 2-МЕ 2-МЕ 200 100 90 75 50 25 20 15 | | |I| | |||
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Q: BSA (mg/ml) Absorbancy 540nm 0.158 1 0.210 2 0.260 3 0.305 4 0.360 5 0.410 0.455 7 0.510 8 0.530…
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Q: Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7…
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- an protein has a molecular wieght of 90 KD when purified by gel filtration and has a molecular wieght of 60 KD hen purified by electrophoresis which one is the more selective?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).A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecularmasses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein.
- 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).You are given a 27 % (w/v) solution of psicose. Molar mass: psicose (C6H12O6) = 180.156 g/mol. ou have a 0.75 mg/mL solution of bovine serum albumin (BSA). You add 1 mL of the 0.75 mg/mL BSA solution into a standard cuvette (1 cm path length), set your spectrophotometer to 280 nm and read the absorbance of this BSA solution. Molecular mass of bovine serum albumin = 66.4 kDa. Molar extinction coefficient (e) of BSA = 43824 M-1 cm-1 (at 280 nm). What absorbance reading will you obtain?Two proteins of different molecular weight (mw) are mixed and need to be separated. When eluted through a Sephadex-G50 chromatography column, what is the order of elution (first followed by second)? A. protein with mw of 40 kDa; protein with mw of 20 kDa B. both proteins will elute at the same time C. both proteins will not elute as the combined mw is larger than 50 kDa D. protein with mw of 20 kDa; protein with mw of 40 kD
- Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?It is necessary to develop a string matching method that may be used to compare two or more proteins. What is the purpose of this? What proof do you have to support your claim?
- As an example, consider albumin, a protein made of a single polypeptide weighing 66,000 daltons (66 kDa). On the other hand, gamma globulin has quaternary structure: is made of four polypeptides, two of which weigh 23,000 daltons (23 kDa) each, and two of which weigh 53,000 daltons (53 kDa) each. When treated with reducing agent and SDS, the subunits separate and they all linearize. If albumin and gamma globulin were run through gel electrophoresis, which polypeptides would move the fastest? Which would move the slowest?After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bonds