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- 6-73 In each case, tell which side (if either) rises and why. The solvent is water. A A Osmotic membrane (a) 1% glucose (b) 0.1 M glucose (c) 1 M NaCl (d) 1 M NaCl (e) 3% NaCl (f) 1 M NaBr (B) B 5% glucose 0.5 M glucose 1 M glucose 1 M K₂SO4 3% KC1 1 M KC1The 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).1. 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
- 7. [10'] For a bacteriophage 77, the following data at zero concentration have been obtained: Sedimentation coefficient: $20,w = 453 S. Diffusion coefficient: D₂0. = 6.03×10-8 cm² s¹¹. 20,w Specific volume V20 = 0.639 cm³ g¹ Calculate the molecular mass M of the bacteriophage.4. A solution containing egg albumin (pl-4.6), B-lactoglobulin (pl-5.2), and chymotrypsinogen (pl=9.5) was loaded onto a column of diethylaminoethyl cellulose (DEAE-cellulose) at pH 5.4.The column was then eluted with a pH 5.4 buffer, with an increasing salt concentration. Predict the elution pattern.1:55 .ll 0.52 KB/S 56 1.pdf CHEM 3141: BioChemistry Quiz no. 1- Answer key I.) Draw the following compounds. 1.) Maltose: 2 Glucose, a-(1,4) 2.) Gentobiose: 2 Glucose, B-(1,6) 3.) C-2 epimer of Talose 4.) C-3 epimer of Fructose 5.) C-2 epimer of ribose II. Predict the products of the following reactions, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow он FO HO -H H -OH но. + Resorcinol/dilute HCI 1.) 2.) Sucrose + Copper (II) Acetate/Acetic Acid HO H HO H HO H H OH 3.) HO + Orcinol/HCI
- 6-One method to determine proximity of two locations in a protein molecule or protein complex is FRET. This technique uses fluorescence transfer between two fluorophores where the ability of the transfer to occur is correlated to distance between the two residues. A) On the following graph using colored pencils, pens, or markers draw the emission spectra from the donor and the absorbance spectra of the acceptor (this should be a general schematic, does not need to be a FRET pair). Include a key for your graph B) As a rescarch student in my group you want to study the proximity of two residues in clamp region of a protein. Draw a schematic of your protein and label the two locations of your fluorophores. In 2-4 sentences (or figures) explain how your FRET fluorophores would give determine if these two residues were close to one another.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.Draw the structure of pentapeptide Trp-Asp-Cys-Lys-Gln that would predominate in aqueous solution at pH=5.5. (Relevant pKa values are 2.2, 3.8, 8.3, 9.6 and 10.5.)
- 2)Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. Which protein would move toward the positive electrode? choose all that applies. Cytochrome C Myoglobin Hemoglobin Serum AlbuminYou 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/mLConsider a negatively charged protein adsorbed on anion-exchange gel at pH 8. (a) How will a gradient from pH 8 to some lower pH be useful for eluting the protein? (b) How would a gradient of increasing NaCl concentration (at constant pH) be useful for eluting the protein?
