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- The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).Suppose you have a mixture of the following proteins protein A: pl = 3.5, mw = 35 kDa protein B: pl = 5.5, mw = 22 kDa protein C: pl = 7.5, mw = 77 kDa protein D: pl = 9.0; mw = 52 kDa. Which protein do you expect to elute last if you perform separation using cation exchange chromatography at pH 7.0? A B OcExplain why it has been very difficult to obtain an X-ray crystal structure for the complete nuclear pore complex. Explain in terms of its size, number of proteins as well as its molecular properties (e.g. charge)
- AH = - 1.2 kcal/mol; Кр 3 16 nM OH 1 HO AH = - 6.0 kcal/mol; Kp = 76 nM OH HOll AH = - 5.5 kcal/mol; Kp = 0.5 nM OH 3 (iv) Consider the molecule 1 being derivatized to yield molecule 2. How would you expect AG for the binding process (to their target) of 2 to compare to 1? Justify your answer.Suppose you have two genetic variants of a large protein that differ only in that one contains a histidine (side chain pK, = 6.4) when the other has a valine (uncharged side chain). (a) Which would be better for separation: gel electrophoresis or iso- electric focusing? Why? (b) What pH would you choose for the separation?A solution contains a mixture of four proteins: urease, ovalbumin, lysozyme, and alkaline phosphatase. The proteins have the following properties. Molecular weight (Daltons) Protein pl Urease 483,000 5.0 Ovalbumin 45,000 4.6 Lysozyme 86,000 11.0 Alkaline 86,000 4.6 Phosphatase Based on the information provided, what type of chromatography (gel permeation or ion exchange) could be used to separate: a) Lysozyme from Alkaline Phosphatase. Briefly explain your answer. b) Ovalbumin from Alkaline Phosphatase. Briefly explain your answer. c) Which of the four proteins would be bound to a cation exchanger equilibrated at pH 5? d) Briefly explain your answer to part c).
- Nonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?2 / 9 100% +| 1. Explain why only small areas of the Ramachandran plot (below) are occupied (shaded grey) and what the two dark grey shaded areas represent in terms of a protein structure. +180 120 60 -60 -120 -180 -180 -120 -60 60 120 +180You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mL
- (a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M 60 113588 65 Temp. (°C) 70 75 80 Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? • To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? ● Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? • Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?. Suppose you have two genetic variants of a large protein that differ only in that one contains a histidine (side chain pk, = 6.0) when the other has a valine (uncharged side chain). (a) Which would be better for separation: gel electrophoresis or isoelectric focusing? Why? (b) What pH would you choose for the separation?In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.