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- Using DEAE-cellulose as ion exchange resin, indicate the starting and ending pH for the narrowest experimental pH range used to separate an amino acid mixture consisting of Gln, Leu and Lys Starting pH: _____ Ending pH: _____You need a buff er at pH 7.5 for use in purifying a protein at 4°C. You have chosen Tris, pK 8.08, ΔH° = 50 kJ · mol−1. You carefully make up 0.01 M Tris buffer, pH 7.5 at 25°C, and store it in the cold to equilibrate it to the temperature of the purifi cation. When you measure the pH of the temperature-equilibrated buff er it has increased to 8.1. What is the explanation for this increase? How can you avoid this problem?NaCl (Mr = 58.443 g/mol) 2.5 M Tris-Cl, pH 8 oplossing / solution (1 Litre) EDTA, sodium salt (Mr = 380.2 g/mol) 10 % Sodium dodecyl sulfate solution Proteinase K solution (50 mg dissolved in 1 ml ddH2O) You need a digestion buffer consisting of the following: 15 mM NaCl 75 mM Tris-Cl, pH 8 16 mM EDTA, pH 8 0.8 % Sodium dodecyl sulfate 0.75 mg/ml proteinase K Calculate: How will you prepare 500 ml of the digestion buffer? Show all your steps and calculations and remember to explain how exactly you will make it up.
- Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank 0 2 0.2 0.12 3 0.4 0.25 4 0.6 0.45 5 0.8 0.55 6 1.0 100 0.68 7 Unknown (0.5ml) 0.41) In urea assay (Catalog #K375-100) what is the nmol (range) it can detect?The concentration of hydrolyzed nitrocefin at each time point for an experiment is given below. Time (min) Concentration (μM) 0.5 6.01 1 11.78 1.5 17.6 2 23.51 2.5 29.58 3 35.31 3.5 39.73 4 44.5 4.5 48.18 5 50.05 5.5 52.72 6 54.01 6.5 55.06 7 55.65 7.5 56.39 8 56.74 8.5 57.49 9 58.03 9.5 58.61 10 58.69 Make a graph that plots the concentration of hydrolyzed nitrocefin (in μM) against time (in seconds) using Excel, R, SPSS or other computable software. Where appropriate, include a trendline that shows the linear range on your graph. Include the equations for the trendlines and the R2 value on the graph. Your graph should also include a title and appropriate titles for the x- and y-axes, with units included where appropriate. To determine the initial velocity of a possible insert in this experiment, you must determine what the linear range is in these data (see note below). Based on your graph, which time points represent a suitable linear…
- A student who was isolating aspirin stopped the experiment after the filtration step with alumina. One week later, the methanol was evaporated and the experiment was completed. The melting point of the aspirin was found to be 110–115°C. Explain why the melting point was low and why the melting range was so wide.Chitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3.
- A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…Biomolecules Reference : https://youtu.be/QB02OJ4zg68You are given as following : 20 µl pure LDH on ice, 2.0ml of 6mM NAD+, 2.0ml of 150mM lactate, and 0.14M CAPS buffer. LDH reaction cocktail has final concentration of 1mM NAD+ and 25mM lactate in 0.14M CAPS buffer. LDH activityis measured by mixing 10 µl of LDH sample and 990 µl LDH reaction cocktail before getting ∆A340/min reading on spectrometer. (a). Describe in detail how you would prepare for your LDH reaction cocktail including how to make dilutions.