CLS570 Part 3 Chemical
Synthesis of peptides +
Peptide Analogues Practice
Questions And Correct
Answers (Verified Answers)
Plus Rationale 2026 2027
Q&A| Instant Download Pdf.
1. What is the fundamental chemical bond linking amino acids in a
peptide?
A. Ester bond
B. Disulfide bond
C. Amide (peptide) bond
D. Ether bond
The peptide bond is an amide bond formed between the carboxyl
group of one amino acid and the amino group of another.
2. Which functional group of an amino acid normally participates in
peptide-bond formation at the N-terminal side?
A. Side-chain methyl group
B. α-Amino group
C. α-Carboxyl group
D. Sulfhydryl group
,The α-amino group reacts with the carboxyl group of another amino
acid during peptide synthesis.
3. In a conventional peptide, the N-terminus refers to the end
containing the:
A. Free carboxyl group
B. C-terminal protecting group
C. Free or functionally available amino group
D. Side-chain hydroxyl group
The N-terminus is the end of the peptide associated with the amino
group.
4. The C-terminus of a peptide contains the:
A. Free amino group
B. Carboxyl group
C. Sulfhydryl group
D. Aromatic ring
The C-terminal residue contains the peptide's terminal carboxyl
functionality.
5. Why are protecting groups commonly required during chemical
peptide synthesis?
A. To increase peptide molecular weight
B. To make amino acids more acidic
C. To prevent unwanted reactions at functional groups that should
remain unreactive
D. To eliminate peptide bonds
,Protecting groups temporarily mask reactive functionalities so
synthesis can proceed selectively.
6. Which protecting group is commonly used to protect the α-
amino group in Fmoc solid-phase peptide synthesis?
A. Boc
B. Cbz only
C. Fmoc
D. Acetyl chloride
Fmoc, or 9-fluorenylmethoxycarbonyl, is widely used as an Nα-
protecting group in SPPS.
7. Fmoc protection is particularly useful because it is removed
under:
A. Strong oxidizing conditions
B. Strongly acidic conditions only
C. Basic conditions
D. Reducing conditions only
Fmoc is base-labile and is commonly removed with piperidine-
containing solutions.
8. What does SPPS stand for?
A. Sequential Peptide Purification System
B. Solid-Phase Peptide Synthesis
C. Synthetic Protein Processing System
D. Side-chain Peptide Protection Scheme
SPPS is the standard abbreviation for solid-phase peptide synthesis.
, 9. In solid-phase peptide synthesis, the growing peptide is attached
to a:
A. Gas phase
B. Liquid solvent molecule
C. Solid support resin
D. Metal catalyst
The peptide remains covalently attached to a resin during iterative
synthesis.
10. One major advantage of SPPS is that:
A. No protecting groups are required
B. Peptides never require purification
C. Excess reagents can be removed by washing the resin
D. Peptide bonds form spontaneously
The solid support permits repeated washing and removal of soluble
reagents and by-products.
11. During conventional Fmoc-SPPS, synthesis generally proceeds
from:
A. N-terminus to N-terminus
B. C-terminus toward N-terminus
C. Side chain to C-terminus
D. N-terminus toward C-terminus
The first residue is attached through its C-terminal carboxyl group to
the resin, and residues are then added toward the N-terminus.
12. The first amino acid loaded onto a typical peptide resin
corresponds to the:
Synthesis of peptides +
Peptide Analogues Practice
Questions And Correct
Answers (Verified Answers)
Plus Rationale 2026 2027
Q&A| Instant Download Pdf.
1. What is the fundamental chemical bond linking amino acids in a
peptide?
A. Ester bond
B. Disulfide bond
C. Amide (peptide) bond
D. Ether bond
The peptide bond is an amide bond formed between the carboxyl
group of one amino acid and the amino group of another.
2. Which functional group of an amino acid normally participates in
peptide-bond formation at the N-terminal side?
A. Side-chain methyl group
B. α-Amino group
C. α-Carboxyl group
D. Sulfhydryl group
,The α-amino group reacts with the carboxyl group of another amino
acid during peptide synthesis.
3. In a conventional peptide, the N-terminus refers to the end
containing the:
A. Free carboxyl group
B. C-terminal protecting group
C. Free or functionally available amino group
D. Side-chain hydroxyl group
The N-terminus is the end of the peptide associated with the amino
group.
4. The C-terminus of a peptide contains the:
A. Free amino group
B. Carboxyl group
C. Sulfhydryl group
D. Aromatic ring
The C-terminal residue contains the peptide's terminal carboxyl
functionality.
5. Why are protecting groups commonly required during chemical
peptide synthesis?
A. To increase peptide molecular weight
B. To make amino acids more acidic
C. To prevent unwanted reactions at functional groups that should
remain unreactive
D. To eliminate peptide bonds
,Protecting groups temporarily mask reactive functionalities so
synthesis can proceed selectively.
6. Which protecting group is commonly used to protect the α-
amino group in Fmoc solid-phase peptide synthesis?
A. Boc
B. Cbz only
C. Fmoc
D. Acetyl chloride
Fmoc, or 9-fluorenylmethoxycarbonyl, is widely used as an Nα-
protecting group in SPPS.
7. Fmoc protection is particularly useful because it is removed
under:
A. Strong oxidizing conditions
B. Strongly acidic conditions only
C. Basic conditions
D. Reducing conditions only
Fmoc is base-labile and is commonly removed with piperidine-
containing solutions.
8. What does SPPS stand for?
A. Sequential Peptide Purification System
B. Solid-Phase Peptide Synthesis
C. Synthetic Protein Processing System
D. Side-chain Peptide Protection Scheme
SPPS is the standard abbreviation for solid-phase peptide synthesis.
, 9. In solid-phase peptide synthesis, the growing peptide is attached
to a:
A. Gas phase
B. Liquid solvent molecule
C. Solid support resin
D. Metal catalyst
The peptide remains covalently attached to a resin during iterative
synthesis.
10. One major advantage of SPPS is that:
A. No protecting groups are required
B. Peptides never require purification
C. Excess reagents can be removed by washing the resin
D. Peptide bonds form spontaneously
The solid support permits repeated washing and removal of soluble
reagents and by-products.
11. During conventional Fmoc-SPPS, synthesis generally proceeds
from:
A. N-terminus to N-terminus
B. C-terminus toward N-terminus
C. Side chain to C-terminus
D. N-terminus toward C-terminus
The first residue is attached through its C-terminal carboxyl group to
the resin, and residues are then added toward the N-terminus.
12. The first amino acid loaded onto a typical peptide resin
corresponds to the:
