Chapter 21: Q10P (page 996)
Calculate the pI of each of the following amino acids:
a.asparagine b. arginine c. serine d. aspartate
Short Answer
(a) pI = 5.43
(b) pI = 10.76
(c) pI = 5.68
(d) pI = 2.98
Chapter 21: Q10P (page 996)
Calculate the pI of each of the following amino acids:
a.asparagine b. arginine c. serine d. aspartate
(a) pI = 5.43
(b) pI = 10.76
(c) pI = 5.68
(d) pI = 2.98
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Get started for freeAlanine has pKa values of 2.34 and 9.69. Therefore, alanine exists predominately as a zwitterion in an aqueous solution with pH > ____ and pH < ____.
a. What percentage of the -amino group of lysine will be protonated at its pI?<25%50% >75%
b. Answer the same question for the-amino group of lysine.
Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50 (Figure 21.3):
a. aspartate before serine c. valine before leucine
b. serine before alanine d. tyrosine before phenylalanine
Explain the difference in the \({\bf{p}}{{\bf{K}}_{\bf{a}}}\) values of the carboxyl groups of alanine, serine, and cysteine.
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride,
trypsin will cleave the polypeptide only on the C-side of arginine.)
Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-
Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp
a. After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine?
b. How many fragments are obtained from the polypeptide?
c. In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
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