1. Hen Egg Lysozyme (HEL) is a commonly studied protein. One study reported that HEL unfolded at a “melting" temperature (TM) of 77.8 °C and calorimetric measurements determined the enthalpy for melting to be 500 kJ/mole. At the melting temperature, what are AG and AS°?
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- A protein gives, under conditions of buffer composition, pH, and temperaturethat are close to physiological conditions, a molecular weight by size exclusion measurements of 140,000 g/mol. When the same protein is studiedby SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits, and the kinds of bonding(covalent, noncovalent) existing between subunits.Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…2. 0.1 mL of a protein solution of concentration of 7 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 3 mL of this solution was then mixed with 27 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
- 3. 4. A protein solution is prepared by dissolving 800 µg of protein in 200 µL of water. A 150 μL sample of this solution is diluted to a total volume of 4.5 mL. How many mg of protein will be in a 3 mL sample of the diluted protein solution? Space to show your workings:If your initial absorbance from undiluted crude dialysate is 4.50, determine the fold dilution needed to yield an absorbance of approximately 0.700. If you want to prepare 1.0 ml of diluted crude, what volume (mL) of crude dialysate must you add? Your Answer: Answer units It is possible to estimate the molar extinction coefficient of a protein from knowledge of its amino acid composition, as shown from your experiences with EXPASY. From the molar extinction coefficient of tyrosine, tryptophan and cystine (cysteine does not absorb appreciably at wavelengths >260 nm, while cystine does) at a given wavelength, the extinction coefficient of the native protein in water can be computed using the following equation: e(Protein) = #(Tyr)*E(Tyr) + #(Trp)*E(Trp) + #(Cystine)*E(Cystine) Where (if A280 measured in water): E (Tyr) = 1490, ɛ (Trp) = 5500, e (Cystine) = 125 Estimate the molar extinction coefficient of lysozyme using the above equation and the amino acid composition data you found…Diethylaminoethyl cellulose is a positively charged resin used in ion-exchange chromatography with a pKa is about 11. A negatively charged protein with an isoelectric point of 5.0 is applied to the column in a buffer at pH 7 and containing 0.1 M NaCl. Which of the following conditions is most likely to weaken the interaction between the protein and the resin? A Raising the pH to 8 and decreasing the NaCl to 0.05 M B Raising the pH to 8 and increasing the NaCl to 0.2 M C Lowering the pH to 6 and decreasing the NaCl to 0.05 M D Lowering the pH to 6 and increasing the NaCl to 0.2 M
- 1. Calculate the approximate MW of a protein with 341 amino acid residues and express it ing/mol and in kD. Show complete solution.A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume. From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme. Explain why ferritin and ovomucoid behave anomalously. Table 1 - The Vel versus Mr data Protein Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column. # Do not…16. A quantitative study of the interaction of a protein with its ligand yielded the following results: Ligand concentration 0.5 1 2 3 4 5 6 9. 12 (μM) v (moles of 0.14 0.31 0.48 0.61 0.68 0.72 0.77 0.79 0.81 ligand bound per mole of protein) Plot a graph of ligand concentration versus v. Determine KD, the dissociation constant for the interaction between the protein and its ligand, from the graph.
- A 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. A protein gives, under conditions of buffer composition, pH, and tem- perature that are close to physiological conditions, a molecular weight by sedimentation equilibrium measurements of 140,000 g/mol. When the same protein is studied by SDS gel electrophoresis in the absence or presence of the reducing agent B-mercaptoethanol (BME), the pat- terns seen, respectively, in lanes A and B are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoi- chiometry of subunits, and the kinds of bonding (covalent, noncova- lent) existing between subunits. / A B - BME + BME STD Serum albumin, 67,000 Ovalbumin, 43,000 Carbonic anhydrase, 30,000 Trypsin inhibitor, 20,000 10 2. 4. Co cm migrated1. Lactoferrin is an iron-binding glycoprotein that forms the antibiotic fragment lactoferricin during digestion. The protein was isolated from 1.5 liters of ewe skim milk by successive ammonium sulfate precipitation until a final salt concentration of 70% was obtained. Determine the amount (in g) of powdered ammonium sulfate needed in bringing the solution from (a) 0% to 40% saturation and (b) 40% to 70% saturation assuming that the volume remains constant. Initial concentration of (NH4)2SO4, % saturation 0 10 20 30 40 50 60 70 80 90 10 55 Final concentration of (NH4)2SO4, % saturation 30 40 50 60 70 80 Grams of solid (NH4)2SO4 to be added to 1 L of solution 176 242 314 390 472 561 657 117 405 491 584 59 421 351 438 20 113 57 182 121 61 251 325 63 188 126 195 130 65 260 337 270 202 281 135 67 210 140 70 90 761 685 511 609 533 365 292 219 146 HUGH LATLE 100 73 457 381 305 228 152 76