1 2 3 4 5 6 N Sample Lysate Name volume 8 Tilapia Cod Sole Perch Tilapia Cod Sole 2 μl Perch 10 με 2 μ. 10 με 2 μl 10 μl [protein] [protein] in in assay lysate 3.9 µg/ml 19.9 µg/ml 18.2 µg/ml > 20 µg/ml 9.4 µg/ml 2 μι 10 με *assay range: 2-20 µg/ml What volume of the each fish "gel-ready" sample should you load on your gel to load 5µg of protein? > 20 µg/ml <2 µg/ml 7.3 µg/ml [protein] volume in to load 5 "gel- ready" μg sample protein 7.3 μl 4.2 μl μg protein in 20 μl 19.5 μl 4.2 μl > <
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- If a protein lysate obtained is 1003 ug/ml What would be the total concentration of each lysate that is loaded into their well if you load just 25 ul of each?A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?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.
- 3 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.Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073xThesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portion
- A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?1.0 ml of serum albumin (BSA) solution was precisely diluted to 100 ml with a buffer solution, and the absorbance at 280 nm was measured from this buffer solution at a distance of 1 cm from the light. The result was A=1.0. BSA is 0.1%(=0.1g/l). The absorptivity is e(0.1%)=0.667, so 1g/l solution gives an absorbance of 0.667. What was the original protein content? Report in the result unit mg/ml with an accuracy of 0.1 mg.A protein required 6.8 min to travel 82 cm to the detector in a 96 cm -long capillary tube with 25.4 kV between the ends. Find the apparent electrophoretic mobility. How many femtomoles of 2.4 μM protein are injected electrokinetically into a 50 μm diameter capillary at 5.0 kV for 3.0 sec. if the sample has half of the conductivity of the background electrolyte.
- 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).What is the approximate rate of change of A340 measured? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 30 ml of the ADH solution was tested in the same way (i.e. half the amount of protein) ? i.e. ΔA340 / min = __________ What rate of change of A340 would you predict if 60 ml of a 0.5 μM ADH solution was tested in the same way? i.e. ΔA340 / min = __________ As well as writing your answers, explain your reasoning.After three minutes, the concentration of drug Zip in the red blood cells is 10 mmoles l-1. What is the average rate of entry of drug Zip into the red blood cells in units of moles min-1 red blood cell-1 during the first three minutes after placing the red blood cells into the bathing solution? Assume that each red blood cell occupies about 1 x 10-13 liters.