Ribbon diagrams show secondary structures and appear less detailed than other model types. In one to two sentences, give a reason that chemists would use ribbon diagrams. What type of information do they provide
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Ribbon diagrams show secondary structures and appear less detailed than other model types. In one to two sentences, give a reason that chemists would use ribbon diagrams. What type of information do they provide?
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- Remember that DNA is a sequence of the letters A,C,T, and G. A binds with T and C binds with G. Solutions are specified by the DNA sequence, such as ACAC or TG, and by the concentration in units of micromolar (uM = 10-M) Consider mixing 30ml of 0.30µM ACAC with 45ml of 0.50pM TG. Predict what reactants and products should be present in the final solution and then check your answer in the virtual lab. (Please give your final answer in total nanomoles (10 moles) for each species in the solution)Suppose you have two genetic variants of a large protein that differ only in that one contains a histidine (side chain pK, = 6.4) when the other has a valine (uncharged side chain). (a) Which would be better for separation: gel electrophoresis or iso- electric focusing? Why? (b) What pH would you choose for the separation?Using a detailed scheme, propose a step-wise protocol to purify protein B by ion exchange chromatography (Explain your logic/choices).
- Give a clear Detailed Solution with explanation needed...(no need Handwritten)2. . questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. Calculate the overall charge (pH 7) on the following three polypeptides and answer the (A) Ser-Tyr-Ser-Met-Glu–His–Phe–Arg-Trp-Gly-Lys-Pro–Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu--Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His–Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu–Phe-Cys-Ser-Tyr-Ser-Met–Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (g) Which of the three peptides would migrate the furthest away from the anode in isoelectric fo- cusing (h) Which of the peptides would migrate the closest to the cathode in isoelectric focusing?…The concentration of protein in a solution can be determined via UV spectroscopy and colorimetry* techniques. Explain further on the statement, give examples of the techniques (please provide three examples for the colorimetry), general principles/mechanism, and general procedures of the techniques. You may use a Table to present the answer. If you need to choose a technique to measure your protein sample, what would be your choice? Justify your answer.
- . Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true[Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.You are working as a Research Scientist I at Albany Molecular Research. For one of your bacterial growth media, you need to prepare 1.4 liters of a 35mM sucrose solution. What do you need to do? MW of sucrose is 342 g/mol Oa. dissolve 168 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters O b. dissolve 8.55 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters c. dissolve 16.8 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters N d. dissolve 14.1 g of sucrose in~ 1 liter and fill total volume to 1.4 liters O e. dissolve 16.8 g of sucrose in 1.4 liters
- Provide differences between solution-phase peptide synthesis and solid phase synthesis in terms of: 1.purification requirements 2.glassware requirements 3.solvent/reagent consumption 4.efficiency and automation 5. protection chemistry requirements 6. peptide coupling chemistryGive Detailed Solution with explanation...(no need Handwritten)H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).