the same 10.00 mL of a 0.5 M NaOH is added to 150.0 mL of MOPS buffer. The buffer contains 0.500M MOPS-H and 0.500 M MOPS. Calculate the new pH after the acid was added. MOPS pka = 7.2 the answer is 7.26 I just want to know how to do it Calculate the charge on the following polypeptide chain at a pH of 5: Arg-Asp-His-Tyr the answer is +1 I just want to know how to do it

the same 10.00 mL of a 0.5 M NaOH is added to 150.0 mL of MOPS buffer. The buffer contains 0.500M MOPS-H and 0.500 M MOPS. Calculate the new pH after the acid was added. MOPS pka = 7.2 the answer is 7.26 I just want to know how to do it Calculate the charge on the following polypeptide chain at a pH of 5: Arg-Asp-His-Tyr the answer is +1 I just want to know how to do it

Appl Of Ms Excel In Analytical Chemistry

2nd Edition

ISBN:9781285686691

Author:Crouch

Publisher:Crouch

Chapter8: Polyfunctional Acids And Bases

Section: Chapter Questions

Problem 14P

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For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?apKa of 3.3. The amino group of alanine has a p?apKa of 8.8. Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7.
Consider the titration of 50.00 ml of a solution of 0.2574 M of the fully protonated form of the diprotic amino acid glycine (pKa1 = 2.34, pKa2 = 9.60) with 0.3786 M KOH. What is the pH after the addition of 33.99 mL of the KOH solution?
Plot the titration curves of valine and lysine amino acids in basic medium and calculate the pI values. valine (pKa1: 2,32; pKa2: 9,62) lysine (pKa1: 2,18; pKa2: 8,95; pKa3:10,53)
You are supplied with the following: 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.
Calculate the pH formed by mixing 35.0 mL 0f 0.0500 M of the neutral form of glutamic acid with 65.0 mL of 0.0400 M NaOH. Ignore the effects of activity. pKa1 = 2.23, pKa2 = 4.42, pKa3 = 9.95
You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Answer the following questions. a. Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculations. Draw the structure of the amino acid at the pH determined in question 1a.
The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in the range of 0.2 to 1.0 mg/ml. For each concentration, a volume of 1.0 mL should be prepared. Describe how you will prepare these standards using a stock solution of BSA that is 2.0 mg/ml.
Properties of a Buffer The amino acid glycine is often used as the main ingredient of a buffer in biochemical experiments. The amino group of glycine, which has a of 9.6, can exist either in the protonated form or as the free base , because of the reversible equilibrium In what pH range can glycine be used as an effective buffer due to its amino group? In a 0.1 m solution of glycine at pH 9.0, what fraction of glycine has its amino group in the form? How much 5 m KOH must be added to 1.0 L of 0.1 m glycine at pH 9.0 to bring its pH to exactly 10.0? When 99% of the glycine is in its form, what is the numerical relation between the pH of the solution and the of the amino group? Please answer all of these questions, especially C please write in detail.
For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?a of 3 The amino group of alanine has a p?a of 8 Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7. __?__x10^?
"A protein has a pI point which can be used to separate proteins using ion exchange. If you have an anion exchange column and access to buffers of any pH, how could you isolate a protein with a pI of 7 from a mixture of proteins which also has proteins with pI points of 3 and 5" Write a few sentences or draw a picture.
a) 75mL of a 0.2M solution of a tripeptide Ser-Cys-His is adjusted to pH=8.6. The solution is then titrated with 50mL of 0.5M HCl. Calculate the new pH value of the tripeptide solution. (Relevant pKa values are: 2.2, 6.0, 8.3, and 9.6). b) Once you've completed the addition of HCl to the tripeptide in part a you then titrate the solution with 30 mL of 0.6M NaOH. Calculate the final pH value of the tripeptide solution.
An enzyme is needed to be stored in a buffer solution with a pH of 10.00. Unfortunately, only three buffer systems are available in their laboratory: Buffer System Weak Acid Component Ka Conjugate Base Salt PAH Benzoic acid, C6H5COOH 6.25 x 10-5 NaC6H5COO SAD Boric acid, H3BO3 5.81 x 10-7 NaH2BO3 DOH Hydrogen cyanide, HCN 6.20 X 10-10 NaCN In what buffer system (PAH, SAD, or DOH) will Phoebe store the enzyme? (show calculations and briefly explain) Write the equilibrium reaction involved in the buffer system. Calculate the amount (in mL) of the 2.00 M stock solution (pH 10.00) of the same buffer system needed to prepare 250 mL of a 0.650 M buffer pH 10.00.