1. Explain why only small areas of the Ramachandran plot (below) are occupied (shaded grey) and what the two dark grey shaded areas represent in terms of a protein structure. +180 120 60 -60 -120 -180 -180 -120 -60 60 120 +180
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- This is an SDS-PAGE gel of the protein insulin. The first lane is the molecular weight standard marker. The second lane NR is the native, non-reduced protein (MW 5.7kDa). The third lane is the protein treated with beta-mercaptoethanol. Please explain what is shown in the NR lane versus the R lane.Marker Proteins Molecular Weight (daltons) Distance 132,000 66,000 43,000 14,400 Serum Albumin (Dimer) Serum Albumin (Monomer) 23mm 32mm Ovalbumin 39mm 60mm Lysozyme Unknown 1 26mm Unknown 2 58mm Rabbit serum (albumin) 33mm 1.On semilog paper (provided below) plot the distance migrated by each standard protein as a function of molecular weight. Determine the molecular weight of the unknown proteins and the major protein found in rabbit serum (albumin) from this calibration curve. ii) Interferon is a protein of 25,000 Dalton. How far would it have migrated, land it been included in this experiment? iii) The average amino acid residue in a protein has a molecular weight of 120 Daltons. Assuming that your unknowns are average, how many amino acid residues do they containA gel filtration column with a fractionation range of 1.5-20 kDa is used to separate out the proteins shown below. If these proteins are collected into separate fractions in between the void volume and total volume, in which order will they elute? Indicate if any of the proteins are found in the void volume or total volume fractions. Protein Z - 3330Da Protein Y - 13kDa Protein X - 1.3kDa I. Total volume fraction II. Third protein fraction III. Second protein fraction IV. First protein fraction V. Void volume fraction
- If you have the same protein loaded in two different lanes of an SDS-PAGE stained with Coomasie blue, and one lane has a darker, thicker band of protein than the other lane, can you say that there is more protein in the lane with the darker band? Why or why not?. You need to prepare 500 μL of a 250 µg/mL bovine gamma globulin solution, for one of your protein standards in the Bradford assay. The available bovine gamma globulin in the lab is in the form of a 2 mg/mL stock solution, and it can be diluted with deionized water. Describe or show below how you would create your desired 250 µg/mL solution.Suppose that you are tasked to determine the protein concentration of an unknown protein solution via Bradford assay. You prepared six solutions of bovine serum albumin (BSA) with different concentrations. The initial concentration of the BSA stock solution is 7.50 mg/mL. Approximately 200 µL of Bradford Reagent was added to each of these solutions and the absorbance at 595 nm was taken after 5 minutes. See the table below for data on the standard solutions. Standard # A595 BSA conc (mg/mL) 0.000 0.158 2 1.125 0.291 2.250 0.372 4 3.375 0.503 5 4.500 6 5.625 0.675 Determine the protein concentration, in mg/mL, of the unknown solution if its absorbance at 595 nm was 0.248. Note: Final answer format must be x.xx (two decimal places). Round off only in the final answer. Do not round off in the middle of calculation.
- AsapKDa 97.4 66.24 45.0 31.0 21.5 14.4 a For each condition (there are 5 different conditions), is there a higher percentage of the total protein in the supernatant, pellet, or is it about equal? For condition 1 - For condition 2 - For condition 3 - For condition 4 - For condition 5 -Proteinase K should be used as the first step of DNA purification (before applying phenol CIA mixture) to remove most proteins. Proteinase K alone cannot remove all proteins from the lysate. Explain why the Proteinase K enzyme cannot remove ALL proteins from the cell lysate.
- You will have to dilute your inital Lysozyme stock in order to pipet volumes larger than 10 uL for the Bradford assay. Calculate a dilution of the 10 mg/mL Lysozyme standard needed to create ensure an appropriate final protein range for the Bradford assay - what concentration will your Lysozyme standard be at for the Bradford assay?C.Why does 500 mM imidazole result in the elution of a protein with a 6X-His tag?A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.