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- 6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.1. Draw the structures of the 20 biologically active AA. Under each structure, write the name, one-letter code, and three-letter code followed by the AA classification based on polarity.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.
- 6a. Using your 5 mg/mL stock solution, you wish to make 100µL of the correct concentration of protein to load. How do you make this working solution? (Yes- you would want this to be in 1x sample buffer, but that makes this question more complicated. So for this question just make the protein in water.) Volume of 10mg/ml Final Volume ! 1 100μL of protein 6b. This is a 1: A N Body* @ 2 W S dilution. #3 X E D $ 4 A C R F B I % 5 T V MacBook Pro U וכ H E U 8 N J ( 0III. Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow. 9.) КОНРЫ(СH-CО)» 10.) Glyoxilic Acid/Conc. H2SO46. Consider the following proteins to answer the questions below: Protein Size (kDa) ε at 280 nm 10 7000 14000 3000 50000 A B C D 50 10 50 pl 4 4 8 8 Red Colored? Yes No No No a. Sketch the UV-Vis spectrum of each pure protein (A, B, C, and D) from 240- 480 nm if they were all present at 20 µM. Note: I want four clearly labeled spectra on one plot.
- 4. Observe the following diagram carefully and answer the following questions. (a) Identify the "B" subunit. Explain its role as a biomolecule. (b) What component does the diagram represent? Briefly mention its function. A NH2 OH в Your answer2. Complete the following for serine, tyrosine, and gylcine. a. Draw the amino acid. b. Circle the side chain. c. Identify whether it is polar, nonpolar, acidic, or basic. d. Look for the pK₁, pk2, and PKR (if there an ionizable side chain) e. At what pH will it exist as a zwitterion? f. What is the range of pH values when it will be positively charged? g. What is the range of pH values when it will be negatively charged?1. A mixture of proteins with the following properties were purified using cation exchange chromatography. Which of the following peaks correspond to the correct protein?Protein M- pI- 11, size- 60 KdaProtein N- pI- 8, size- 112 KdaProtein O- pI- 6, size- 280 KdaProtein P- pI- 4, size- 36 Kda[N.B: I was trying to upload pictures, but it was interrupting, Peak C is the highest peak, Peak D is lowest, Peak B is higher than D; however lower than C and A, Peak A is lower than C only, higher than B and D] a) Peak A is P b) Peak C in N c) Peak D is P d) Peak B is O e) Peak A is M 2. Which transition state analog is the most effective competitor for serine protease such as Chymotrypsin?a) R-C=O-NH-R’b) R-C=O(CH3)-NH-R’c) R-CH(OH)-CH(NH2)-R’d) R-CH(OH)-NH-R’e) R-CH=NR’ 3. If a 14C fatty acid labelled with C14 is fed to a cow, after 30 minutes of Beta oxidation, where will the C14 be found?a) Acetyl coA b) Propionyl coA c) Glutamine d) Glucose 4. How many carbons will…
- 4. Exhibit 4A The following question(s) refer to this peptide: Cys-Ala-Gly-Arg-Gln-Met Refer to Exhibit 4A. The overall, net ionic charge on this peptide at pH = 7 would be: A. +2 B. +1 C. 0 D. -1 E. -220. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?The amino acid shown below has an ionizable side chain with a pka of 4. When this amino acid is in a more basic solution (i.e., pH 11), it would resemble ionization state C and have a charge of -1 HO OH NH₂ lonization state A NH3 lonization state C HO OH NH3+ Ionization state B dyb NH₂ lonization state D