8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. lutian bu the
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- 1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the 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. (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-GIn– 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 (d) Which of the three peptides would migrate the closest to the anode in isoelectric focusing? (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three…2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the 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. (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 (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
- 2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the 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. (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 11. - - I C'IL- - 1! (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three peptides would migrate the slowest on SDS-PAGE (g) Which of the three…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 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?Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.
- Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K (pKa = %3D %3D %3D %3D 10.5) O +2 O+1 O-1 00
- 1. Define proteins 2. Discuss the different properties of proteins 3. Discuss the classification proteins based on the structure of protein 4. Discuss the classification proteins based on composition 5. Discuss the classification proteins based on functions 6. Discuss the solubility of protein in water 7. Discuss the denaturation and renaturation 8. Discuss the protein metabolism 9. Discuss the chemical properties of protein 10. Define amino acids 11. Discuss the non-essential and essential amino acids2. Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0%3; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (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 (h) Which of the peptides would migrate the closest to the cathode in isoelectric focusing? (i) Which of the three peptides would migrate the furthest away from the cathode in isoelectric focus-…Give the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 B