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Chapter 21: 21-50P (page 1026)

Show the peptides that would result from cleavage by the indicated reagent:

a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A

b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide

c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin

Short Answer

Expert verified
  1. Val-Arg-Gly-Met-Arg-AlaSer
  2. Ser-Phe-Lys-Met Pro-Ser-Ala-Asp
  3. ArgSer-Pro-Lys Lys Ser-Glu-Gly

Step by step solution

01

Specificity of carboxypeptidase A in protein cleavage

Carboxypeptidase A is specific to breaking the C-terminal amino acid. Therefore, the bond-breaking sites are:

Val-Arg-Gly-Met-Arg-Ala*-Ser

02

Specificity of cyanogen bromide in protein cleavage

Cyanogen bromide hydrolysis is on the C side of a Met. Therefore, the site of bond breaking is represented by *:

Ser-Phe-Lys-Met*-Pro-Ser-Ala-Asp

03

Specificity of trypsin in protein cleavage

Trypsin hydrolysis is the C-side of Arg and Lys. Therefore, the breaking of the bond takes place after Arg and Lys make three chain.

Arg*-Ser-Pro-Lys*-Lys-Ser-Glu-Gly

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Most popular questions from this chapter

Cells can also convert a-keto acids into amino acids, but because the reagents organic chemists use for this reaction are not available in cells, they carry out this reaction by a different mechanism

(a) What amino acid is obtained from the reductive amination of each of the following metabolic intermediates in a cell by reductive amination?

(b) What amino acids are obtained from the same metabolic intermediates when the amino acids are synthesized in the laboratory?

alpha- Amino acids can be prepared by treating an aldehyde with ammonia/trace acid, followed by hydrogen cyanide, followed by acid-catalyzed hydrolysis.

a. Draw the structures of the two intermediates formed in this reaction.

b. What amino acid is formed when the aldehyde that is used is 3-methylbutanal?

c. What aldehyde is needed to prepare isoleucine?

a.Which amino acid has the lowest pI value?

b.Which amino acid has the highest pI value?

c.Which amino acid has the greatest amount of negative charge at pH = 6.20?

d.Which amino acid has a greater negative charge at pH = 6.20, glycine or methionine?

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

a. Which isomer—(R)-alanine or (S)-alanine—is d-alanine?

b. Which isomer—(R)-aspartate or (S)-aspartate—is d-aspartate?

c. Can a general statement be made relating R and S to d and l?
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