Calculate the approximate MW of a protein with 341 amino acid residues and express it ing/mol and in kD. Show complete solution.
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1. Calculate the approximate MW of a protein with 341 amino acid residues and express it ing/mol and in kD. Show complete solution.
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- q44 please calculate the unknown concentration of the protein A wih an absorbance value of A188 given the standard curve indicated in the table. write your answers in numbers only with 2 decimals. protein concentration (ug/ml) absorbance 0 0.000 0.02 0.161 0.04 0.284 0.06 0.438 0.08 0.572 0.10 0.7623 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.Using the data in Table calculate the average amino acid residue weight in a protein of typical composition. This is a useful number to know for approximate calculations
- 1..Calculate the number of kcal and amount of protein provided by the following formula: 500 mL of 50% dextrose and 1 liter of a 10% amino acid solution. If 250 mL of a 20% intravenous fat emulsion were added, how many more kcal would be provided?5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?For the amino acid arginine: Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. Provide labels (A, B, C, etc.) for each form. b. Calculate the IpH of the amino acid. c. At what pH range(s) it can act as a buffer? d. What will be the predominant form(s) of the amino acid at pH (i) 1.5; (ii) 3.0; (iii) 4.5; (iv) 6.0; (v) 7.5 and (vi) 9.0?
- 2. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (ΔΔGfold = ?). Please help me find out deltadelta G fold.A 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
- Suppose you have a concentration of 356ng/uL for Sample A. How many ng of protein will that be?4.3 Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.1. The hydropathic index represents the sum of hydrophobic and hydrophilic residues of a polypeptide. A.true B.false