64 kDa, Tetramer (a B)2 32 kDa, Dimer αβ 16 kDa, Monomer or B a Elution Volume (mL) Absorban ce at 280 nm
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Hemoglobin is considered to be a tetrameric complex with a 64 kDa (α β)2. When attempting to purify hemoglobin, we must first purify the α and β monomers (about 16 kDa each) to prepare the tetramer. This is formed from the dimer intermediate: 2 α + 2 β -> 2 αβ -> (α β)2. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin tetramer
Using the size-exclusion chromatogram given,
1. Draw an SDS-Page Gel with a reducing agent such as BME using the three peaks listed on the graph.
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- NAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12What is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).Given Poly-L-Lysine and Epsilon Poly-L-Lysine, which polymer(s) can easily dissolve in a saline solution with a pH=7 and at room temperature.
- Lefer to the figure showing the molecular structure of dimethylmercury. H–C-Hg C-H H. Exposure of human skin to a single drop of dimethylmercury can lead to death, as it is highly poisonous and passes easily cell membranes. Based on its structure, why is it able to pass so easily through cell membranes? I-0-I IICIHAn allosteric enzyme is purified and determination of its mass by gel-filtration chromatography yields 240 kDa. Chromatography in the presence of 6M urea yields a 30 kDa species and 90 kDa species. SDS-PAGE in the presence of Beta mercaptoethanol reveals 2 protein bands of 30 kDa and 45kDa. Describe the quatranary structure.In the space provided, draw a Haworth projection for the beta anomer of the following monosaccharide Fischer projection. CHO HO-C-H HO-C-H HO-C-H H-C-OH CH,OH
- 80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.The order is for Moxam 5 gm IM every 8 hours. On hand is 10 gram of Moxam with the following directions. Add 8 mL of diluent to yield 10mL of reconstituted solution. How many mL will you give?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?
- 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.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 NexAla-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a. pH 1.5 b. pH 8 c. pH 13