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You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached.
a. What type of protein-protein interaction do these results suggest?
b. What amino acids are most likely involved in this interaction? (Guess based on assay)
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Solved in 2 steps
- Arginine 12 14.0 VI 12.0F 12.0 10.0F IV 10.0 8.0 8.0 pH 6.0 6.0 4.0- 4.0 2.0 2.0 0.0 0.5 1.0 1.5 2.0 2.5 3.0 Eguiyslonts of Ou Below you can find the titration curve for arginine. The pH was monitored, and the results were plotted as shown in the graph. The key points in the titration are designated I to VI. For each of the statements (a) to (f), identify the appropriate key point in the titration. (pKa (СООН): 1.82, рКa (NH2): 8.99, pKa (R): 12.48) Average net charge of +2 predominates: The predominant species is +H3N-CH-((CH2)3-NH-C-NH2-NH2+)-COO- : Average net charge of arginine is 0: d. а. b. C. The pH is equal to the pka of the carboxyl group: Half of the backbone amino groups are protonated: Average net charge of arginine is +1/2: The carboxyl group has been completely titrated: е. f. g.The proteins given below are separated using CM cellulose at pH 7.0 Write the order of elution of these proteins from the column Proteins pl Fibrinogen 5.8 Hemoglobin 7.1 Lysozyme 11.0 Pepsin 1.0 Ribonuclease 7.8Given 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/ 2D gel electrophoresis?
- Beta-tubulin has a molecular mass of 55 kDa, Approximately how many amino acids are found in Beta-tubulin? O 45 O 450 O 4,500 O 45.000 O 450.000250uL convert to LJoshua needs 150mL of 1X TBE buffer. The stock of TBE Buffer is 15X. How much 15X TBE buffer should he use to make 150mL 1X TBE buffer? O 5mL 25mL O 10mL O 15mL O 20mL O o o o
- Hd 12 10 8 CO 6 st 4 2 0 0 0.5 not text. only, no text. only, no text. 1 1.5 NaOH Equivalents 2 2.5 You create this titration curve of an amino acid. How many buffering zones are there? Enter a number, no letters. 3 A What is the pka1 of this amino acid? Enter only digits What is the pka2 of this amino acid? Digits A A/ What is the pl of this amino acid? Digits A/Table 1.1 Name pK2 pKR Glycine Alanine 2.4 2.3 9.8 9.7 Valine Leucine 2.3 2.4 9.6 9.6 Isoleucine 2.4 9.7 Methionine 2.3 9.2 Phenylalanine Proline Serine 1.8 9.1 2.0 2.1 10.6 9.2 Threonine 2.6 10.4 Cysteine Asparagine Glutamine Tyrosine Tryptophan Aspartate Glutamate 1.8 10.8 8.3 2.0 8.8 2.2 9.1 2.2 9.1 10.9 2.4 9.4 2.0 10.0 3.9 2.2 9.7 4.3 Histidine 1.8 9.2 6.0 Lysine Arginine 2.2 9.2 10.8 1.8 9.0 12.5 ii) Calculate the pI value of aspartate. (iii) Calculate the pI value of arginine.250uL convert to mL
- At pH 10, [OH-] is— 10 M 5 M 10-10 M 10-4 M 0.0000001 MCalculate the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH pH 3.5 4.5 5.5 6.5 7.5 8.5 Dilution Factor 5 5 5 50 50 50 Absorbance 0.098 0.027 0.068 0.028 0.032 0.054Given 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 using SDS page?