The following structure is drawn in an unconventional manner.

(a) Label the N terminus and the C terminus.

(b) Label the peptide bonds.

(c) Identify and label each amino acid present.

(d) Give the full name and the abbreviated name

Short Answer

Expert verified

Peptide bonds are denoted by asterisk (*)

Step by step solution

01

Step-1: Explanation to part (a)

N-terminus is referred to as the free amine end of the peptide chain and free carboxylic acid end is referred to as the C-terminus. Both the termini are different from each other with respect to chemical properties.

02

Step-2: Explanation to part(b)

Peptide bonds are formed when the amine group of one amino acid forms bond with carbonyl carbon of another amino acid. A chain of amino acids is known as polypeptide.

Peptide bonds are denoted with asterisks (*)

03

Step-3: Explanation to part(c)

Amino acids are building blocks of protein molecules. Proteins are broken or digested down into smaller molecules known as amino acids.

04

Step-4: Explanation to part (d)

Full name of the given polypeptide is glycylglutaminylisoleucinamide. Its abbreviated name is Gly-Gln-Ile. Naming of the polypeptide is done from N-terminus to C-terminus.

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Most popular questions from this chapter

Histidine is an important catalytic residue found at the active sites of many enzymes. In many cases, histidine appears to remove protons or to transfer protons from one location to another.

(a) Show which nitrogen atom of the histidine heterocycle is basic and which is not.

(b) Use resonance forms to show why the protonated form of histidine is a particularly stable cation.

(c) Show the structure that results when histidine accepts a proton on the basic nitrogen of the heterocycle and then is deprotonated on the other heterocyclic nitrogen. Explain how histidine might function as a pipeline to transfer protons between sites within an enzyme and its substrate.

Although tryptophan contains a heterocyclic amine, it is considered a neutral amino acid. Explain why the indole nitrogen of trytophan is more weakly basic than one of the imidazole nitrogens of histidine.

Use resonance forms to show delocalization of the negative charge in Ruhemann’s purple anion.

Lipoic acid is often found near the active sites of enzymes, usually bound to the peptide by a long, flexible amide linkage with a lysine residue.

(a) Is lipoic acid a mild oxidizing agent or a mild reducing agent? Draw it in both its oxidized and reduced forms.

(b) Show how lipoic acid might react with two Cys residues to form a disulfide bridge.

(c) Give a balanced equation for the hypothetical oxidation or reduction, as you predicted in part (a), of an aldehyde by lipoic acid.

Show how the following amino acids might be formed in the laboratory by reductive amination of the appropriate α-ketoacid.

Phenylalanine (b) Cysteine (c) Serine (d) Alanine

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