Chapter 21: Q34P (page 1010)
Show the steps in the synthesis of the tetrapeptide Leu- Phe- Ala- Val
Short Answer
The answer is:
Step 1
Step 2
Step 3
Chapter 21: Q34P (page 1010)
Show the steps in the synthesis of the tetrapeptide Leu- Phe- Ala- Val
The answer is:
Step 1
Step 2
Step 3
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Get started for freeExplain why the pI values of tyrosine and cysteine cannot be determined by the method described on page 995.
The aldonic acid of D-glucose forms a five-membered-ring lactone. Draw its structure.
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?
What amino acid is formed using the N-phthalimidomalonic ester synthesis when the following alkyl halides are used in the third step?
(a)
(b)
Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.
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