Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Myoglobin 7.0 16.7 Does all proteins separated properly w/ isoelectric focusing?
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- Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains, arranged as two dimers of αβ. In Sickle Cell Disease, both β-globin chains are altered in the dimers (αβS/αβS). Q3: Which level of structure does the αβ/αβ and αβS/αβS in HbA and HbS describe?The primary structure of mammalian hemoglobin, an a202 tetramer, is approximately. O 2% 18% Ο 50% Ο 78% 0 986 identical to myoglobinA 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.
- Which peptide would absorb the most UV light at 280nm? (Can you show work because I mainly want to know how to solve this type of problem. Thank you!)Leu-Trp-Tyr-Ala Tyr-Lys-Tyr-Cys Glu-Tyr-Ile-Arg Ala-Trp-Trp-Ala Thr-Ala-Ile-ThrA 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?Compute for the albumin to globulin (A/G) ratio using these data given Albumin= 51.9g/L Total protein = 75.5 g/L Note: answer should be in ratio form
- 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.What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weightYou are given a 27 % (w/v) solution of psicose. Molar mass: psicose (C6H12O6) = 180.156 g/mol. ou have a 0.75 mg/mL solution of bovine serum albumin (BSA). You add 1 mL of the 0.75 mg/mL BSA solution into a standard cuvette (1 cm path length), set your spectrophotometer to 280 nm and read the absorbance of this BSA solution. Molecular mass of bovine serum albumin = 66.4 kDa. Molar extinction coefficient (e) of BSA = 43824 M-1 cm-1 (at 280 nm). What absorbance reading will you obtain?
- Avidin exists as a protein complex of around 68 kDa. Research to determine the types of interactions that hold the avidin complex together. Based on your research, which molecular weight would you expect for avidin when treated with beta-mercaptoethanol and run through a native gel? 35 kDa 68 kDa 10 kDa 19 kDaSome characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 75,000 5.0 No 2 12,500 4.8 No 3 73,000 9.8 Yes a. What type of chromatography separates proteins based on their size? b. What type of chromatography separates proteins based on their charge? c. Could gel filtration chromatography be used to separate a mixture containing Protein 2 and 3? Clearly explain why or why not. If gel filtration chromatography can be used to separate Protein 2 from Protein 3, which protein would elute first (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins (Protein 2 and Protein 3) be monitored at 280nm and 400nm (clearly explain)? d. Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by…