Aspartic acid: pKa1: 1.88; pKa2: 9.60; pKa 3: 3.65(side chain)
pI: 2.77. (have carboxyl, amino and side chain groups
a) At pH 1 charge will be +1 because aspartate remain protonated at carboxyl, amino ends and also at side chain.
b) At pH 3.0 charge will be neutral because aspartate gets Deprotonated at carboxyl, but remain protonated at amino end and at side chain.
c) At pH 6.0 charge will be -1 because aspartate gets Deprotonated at carboxyl and at side chain but remains protonated at amino end.
d) At pH 11.0 charge will be -2 because aspartate gets Deprotonated at carboxyl, amino end and also at side chain.
biochem question 9. Determine the net charge of the predominant form of Asp at (a) pH...
1-The net charge of the the tripeptide Asp-Asp-Asp at pH 1.00? a. 0 b. -3 c. -4 d. +1 e. -2 2-The net charge of the tripeptide Asp-Asp-Asp at pH 12.00 ? a. 0 b. -3 c. -4 d. +1 e. -2 How to calculate?
1. The amino acid structures as shown in lecture are the predominant forms at physiological pH (7.4). a. Draw the predominant form of valine when the pH = 7.4 b. Draw the predominant form of valine when the pH = 1.0 c. Draw the predominant form of valine when the pH = 12.0 d. What is the total charge of the predominant form of valine when the pH = 7.4? e. What is the total charge of the predominant form...
biochemistry please show work and check work
5. Indicate the approximate net charge on an asp molecule at each of the followin PH Net Charge 1.0 7.0 b) Draw the structure of the ionic form of asp at pH 12.
Biochem help 2
14. What would be the net charge on the dipeptide Ser-His at pH- 6.04? (Choose the one best answer.) a) 1.5 b) +1; c) +0.5 d) 0 e) -0.5; 15. The pKa of a lysine side chain in a protein ending up on the outside of a globular protein has a different pKa than if the lysine is buried within the interior of a protein. What would be the expected pKa of a side chain of lysine...
biochem question
. Aspartame is an artificial sweetener that is a dipeptide composed of Asp-Phe in which the carboxyl terminus is modified by attachment of a methyl group. Draw the structure of aspartame at pH7. (4 marks) b. Calculate the isoelectric point (PI) for Aspartame. (2 marks) C. At a pH of 10 what form of ion exchange chromatography would be most appropriate to isolate Aspartame? Explain (2 marks) 2) Complete the Venn diagram with respect to the given Kd...
Which is the predominant form of the amino acid serine at pH =1 ? А HOCH, CHCO *NH çao B 9. COCH=CHCOH NH HOCH, CHČO NH sçues D носненсон NH ОА Ос OD
8. Choose the most predominant form of tyrosine in a solution of pH = 9.5? or and on London 9. Draw the major product of the following Hofmann elimination. NH CH3-1 1. Ag20, H20 excess 2. heat ? CHIN 10. Complete the following synthesis by selecting from the list of 10 reagents below. Each reagent (or set of reagents) is labeled as a letter. In the answer box, simply place the order of reagents used as uppercase letters. For example,...
Determine the concentration of H in each solution at 25°C. A solution with pH = 3.0. A solution with pH = 6.0. A solution with pOH = 11.0.
It is important to understand the overall net charge on a molecule at a specific pH, especially when carrying out native gel electrophoresis. At pH 9.5, what will be the predominant form of the amino acid lysine? Draw the structure that best represents your answer. Note: pka1 = 2.18, pka2 = 8.95, pkaR = 10.53
Question 5 (8 Points) Identify the location and type of charge on the hexapeptide Lys-Ser-Asp-Cys-His-Tyr at each of the following pH values: a. pH = 1 b. pH = 5 c. pH = 7 d. pH = 12