Which nuclear isotope used in protein NMR spectroscopy is the most sensitive to detect? Briefly explain why.
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Which nuclear isotope used in protein NMR spectroscopy is the most sensitive to detect? Briefly explain why.
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- What is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you
- Chemistry You have constructed a standard curve from BSA protein for a Bradford Assay. The curve has 0, 1, 2, 3, and 4 ug protein in 50 µl water. You have an unknown protein with concentration somewhere between 1-5 mg/mL. What serial dilution series should you use to guarantee at least two dilutions of your unknown fall below 3 ug (linear portion) on the standard curve? For example, would 1/2 x 1/2 x 1/2 (3 2-fold dilutions) be sufficiently dilute that two of the dilutions would give values within the linear portion of the standard curve?You have purified Protein 'X' and you want to know its concentration. As we learned, you can calculate concentrations by simply measuring UV280 absorbance of protein solutions. Using a UV spectrophotometer, you measured an absorbance of 0.6. Given that Protein X has an absorptivity (or extinction coefficient) of 0.2 mL•mg-cm at 280 nm, what is the concentration of purified protein solution (assume the light path is 1 cm)? -1 O A. 3 g/mL B. 3 mg/mL OC.0.2mg/mL OD.0.2 g/mL OE. 0.6 g/mLCan Hydrophobic Interaction Bead Chromatography be used to isolate Protein X from muscle tissue if Protein X contains many hydrophobic regions? Explain the process of how to isolate Protein X from muscle tissue.
- (b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.Suppose you have a mixture of the following proteins protein A: pl = 3.5, mw = 35 kDa protein B: pl = 5.5, mw = 22 kDa protein C: pl = 7.5, mw = 77 kDa protein D: pl = 9.0; mw = 52 kDa. Which protein do you expect to elute last if you perform separation using cation exchange chromatography at pH 7.0? A B OcConsider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
- For backbone assignments of a medium-size protein (~15kD), CBCA(CO)NH and HNCACB experiments need to be run on an NMR sample. Briefly describe the conditions of protein sample labeling and NMR sample. ?In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.The purification continues with a cation exchange step in which the positively charged cytochrome C protein is separated from negatively charged DNA and other proteins. The cation exchange eluate (volume of solution collected) had a total volume of 42.0 mL and a 1.0 mL aliquot was set aside for further analysis. The following data was obtained from the 1.0 mL aliquot to quantify the protein amount and purity: The absorbance at 410 nm of the aliquot was diluted 5-fold was 0.474 (1 cm pathlength). The absorbance at 595 nm from a 1.0 mL Bradford Assay solution that was diluted by 100-fold from the aliquot was 0.195 (1 cm pathlength). Using the information given, Calculate the total protein amount in mg from the absorbance at 595 nm. Calculate the cytochrome C amount in mg from the absorbance at 410 nm using Beer’s Law.