You need to make a protein buffer of: 100 mM NaCl ⚫ 25 mM Tris 8 • • 5% w/v glycerol 2 mM DTT Your stock solutions are: • 5 M NaCl • 2 M Tris 8 •70% w/v glycerol • DTT @ 154.25 g/mol How would you make a 1L protein buffer Solution? Show your work and describe.

A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G 3

Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.

Acetic acid is the principal ingredient in vinegar as shown; that's why it tastes sour. At equilibrium, a solution contains [CH3CO2H] = 0.0787 M and [H3 O+] = [CH3 CO2−] = 0.00118 M. What is the value of Ka for acetic acid?

can someone explain these calculations to me?

What is the boiling point of 0.800 m lactose in water?(Kb for water is 0.512°C/m)°C

Consider a crude extract with a mixture of the 5 proteins listed below. Protein A 4.5 pl 160 molecular weight, kDa Protein B 12.5 pl and 65 molecular weight Protein C 5.0 pl, 15 molecular weight Protein D 6.8 pl, 150 molecular weight Protein E 9.5 pl, 45 molecular weight You load this protein mixture onto an anion exchange column at pH 11. Next, you apply a "washing" step by passing through buffer at pH 11. Finally, for your elution step, you apply a pH gradient starting from pH 11 to pH 2.0 (A gradient buffer system allows you to gradually and continuously change the pH of your mobile phase starting from pH 11 up to pH 2). You load this same protein mixture onto a Size Exclusion column. Please indicate the order in which these proteins will elute for both. Group of answer choices Yes or No, please explain your answer. If your protein of interest is protein A, would using anion exchange column be completely successful at separating it from all the other proteins? Group of answer…

In an experiment to determine the degree of saturation in 0.43 g of an unknown lipid, the following results were obtained: 1) Total mmole I added to the lipid sample: 3.13 2) mmole I left after incubation (after one hour in the dark cupboard): 0.816 How many mg of I has bound to the lipid sample? Select one: a. 587 b. 2.94e5 c. 2 d. 294 e. 5.87e5

Draw the Mchelis Menton plot  and the Line Weaver Burk Plot using the data given below and find the Vmax and Km from the Plot.

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