Given the figure below. Which structure is predominant at pH = 8.0? %3D
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- 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…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?Which of the following is TRUE, if the protein pH is electrically neutral? Refer to the graph below. a. The denaturation of protein is lower than 100% b. The denaturation of protein is greater than 100% c. The protein is in native form d. The protein is completely denatured
- The pH of the amino acid shown below is:Explain the importance of isoelectric point in proteins in the given data belowAnalyze the image that is given below and focus on the red arrow to be able to answer the questions. Type of Bond: Choices: H-bond Electrostatic Interaction Hydrophobic bond Disulfide bond Peptide bond Level of Protein structure: Choices: Primary Secondary Tertiary Quaternary Method/s of denaturation. CHECK ALL THAT APPLY Heating to 100 degrees Celsius Addition of nitric acid Reaching Isoelectric point Addition of mercuric chloride Addition of sulphosalicylic acid Addition of alcohol Addition of ammonium sulfate
- A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…Explain Four Levels of Protein Structure with examples and talk about the importance of each structure (Primary, Secondary, Tertiary, and Quaternary structure). With photos pleaseplease draw anr label the 20 amino acids found in proteins as they would exist in an aqueous solution at pH=7.4
- (E) Consider an amino acid that has one -amino group (pKa = 9.2), one -carboxyl group (pKa = 1.7) and one ionizable side chain (pKa = 6.2). At which pH range/s would this amino acid be effective as a buffer? If the amino acid shows a net charge of -1 at pH 11 and a net charge of +1 at pH 4, what pKa values would you use to calculate the isoelectric point? At what pH would the net charge be equal to zero?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.Analyze the image that is given below and focus on the yellow arrow to be able to answer the questions. Type of Bond: Choices: H-bond Electrostatic Interaction Hydrophobic bond Disulfide bond Peptide bond Level of Protein structure: Choices: Primary Secondary Tertiary Quaternary Method/s of denaturation. CHECK ALL THAT APPLY Heating to 100 degrees Celsius Addition of nitric acid Reaching Isoelectric point Addition of mercuric chloride Addition of sulphosalicylic acid Addition of alcohol Addition of ammonium sulfate