Organic Chemistry: Amines and Biological Molecules Flashcards

Explain properties and reactions of amines and biological molecules. (102 cards)

1
Q

What type of organic compound contains the functional group –NH2?

A

Primary Amine

Amines are derivatives of ammonia where hydrogen atoms are replaced by alkyl or aryl groups.

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2
Q

What type of amine is formed when ammonia reacts with a halogenoalkane?

A

Primary amine

The halogen atom is replaced by an –NH2 group.

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3
Q

Fill in the blank:

Reaction of a halogenoalkane with ammonia is an example of _______ substitution.

A

nucleophilic

Ammonia acts as a nucleophile donating a lone pair.

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4
Q

True or False:

Nitriles can be reduced to form primary amines.

A

True

Reduction adds hydrogen across the C≡N bond.

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5
Q

What functional group must be reduced to convert a nitrile into a primary amine?

A

Nitrile group

The –C≡N group is reduced to –CH2NH2.

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6
Q

Fill in the blank:

The reduction of nitriles to amines requires the addition of _______.

A

hydrogen

The triple bond is reduced to a single bond.

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7
Q

True or False:

Aromatic amines can be prepared by reducing nitro compounds.

A

True

The nitro group (–NO2) is converted to an amine group (–NH2).

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8
Q

What type of compounds are aromatic amines commonly used to manufacture?

A

Dyes

Many synthetic dyes are produced from aromatic amines.

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9
Q

Fill in the blank:

The nitro group in aromatic compounds is represented as _______.

A

–NO2

Reduction converts it to –NH2.

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10
Q

What reagent is commonly used to reduce nitro compounds to aromatic amines in the laboratory?

A

Tin and hydrochloric acid

The amine is then released by adding alkali.

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11
Q

True or False:

Ammonia acts as a nucleophile when reacting with halogenoalkanes.

A

True

It donates a lone pair of electrons to the carbon atom.

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12
Q

Why are aromatic amines important in industrial chemistry?

A

Dye manufacture

They are key intermediates in producing coloured compounds.

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13
Q

What type of chemical behaviour do amines exhibit in aqueous solution?

A

Weak bases

Amines accept protons using the lone pair on the nitrogen atom.

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14
Q

What particle allows amines to act as bases?

A

Lone pair on nitrogen

The lone pair can accept a proton (H+).

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15
Q

Fill in the blank:

Amines act as bases because the nitrogen atom has a _______ pair of electrons.

A

lone

This pair can bond with H+ to form an ammonium ion.

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16
Q

True or False:

Amines react with acids to form ammonium salts.

A

True

The amine accepts a proton from the acid.

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17
Q

Which compound is generally the weakest base: ammonia, primary aliphatic amine, or primary aromatic amine?

A

Primary aromatic amine

Delocalisation of the lone pair reduces its availability.

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18
Q

True or False:

Primary aliphatic amines are stronger bases than ammonia.

A

True

Alkyl groups donate electron density to nitrogen.

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19
Q

Fill in the blank:

Alkyl groups increase the basic strength of amines by _______ electron density to nitrogen.

A

donating

This makes the lone pair more available to accept a proton.

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20
Q

Why are aromatic amines weaker bases than aliphatic amines?

A

Lone pair delocalisation

The lone pair interacts with the benzene ring π system.

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21
Q

True or False:

In aromatic amines, the nitrogen lone pair is partially delocalised into the benzene ring.

A

True

This reduces its ability to bond with H+.

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22
Q

Fill in the blank:

When an amine accepts a proton, it forms an _______ ion.

A

ammonium

The nitrogen atom gains a positive charge.

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23
Q

What factor mainly determines the basic strength of amines?

A

Availability of lone pair

The more available the lone pair, the stronger the base.

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24
Q

Why do primary aliphatic amines act as stronger bases than aromatic amines?

A

Electron-donating alkyl groups

Alkyl groups increase electron density on nitrogen.

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25
Why are **amines** able to act as **nucleophiles in organic reactions**?
Lone pair on nitrogen ## Footnote The nitrogen atom can donate its lone pair to an electron-deficient carbon.
26
What type of **reaction** occurs when **ammonia reacts with a halogenoalkane**?
Nucleophilic substitution ## Footnote The nucleophile replaces the halogen atom in the molecule.
27
# Fill in the blank: In **nucleophilic substitution with halogenoalkanes**, ammonia acts as a _\_\_\_\_\_\_.
nucleophile ## Footnote It donates a pair of electrons to the carbon atom.
28
# True or False: **Ammonia reacting with a halogenoalkane** initially forms a **primary amine**.
True ## Footnote The halogen is replaced by an –NH2 group.
29
What **product** forms when a **primary amine reacts further with a halogenoalkane**?
Secondary amine ## Footnote The nitrogen becomes bonded to two alkyl groups.
30
# True or False: Reaction of **amines with halogenoalkanes** can lead to **quaternary ammonium salts**.
True ## Footnote Repeated substitution replaces all hydrogen atoms on nitrogen.
31
# Fill in the blank: A **nitrogen atom bonded to four alkyl groups** forms a _\_\_\_\_\_\_ ammonium ion.
quaternary ## Footnote These ions carry a permanent positive charge.
32
What **industrial application** commonly uses **quaternary ammonium salts**?
Cationic surfactants ## Footnote They are used in detergents, disinfectants and fabric softeners.
33
# True or False: **Ammonia** can react with **acyl chlorides to form amides**.
True ## Footnote The chlorine atom is replaced by an –NH2 group.
34
# Fill in the blank: The **reaction of ammonia with an acyl chloride** produces an _\_\_\_\_\_\_.
amide ## Footnote The product contains the –CONH2 functional group.
35
What type of **mechanism** occurs when **amines react with acyl chlorides**?
Nucleophilic addition–elimination ## Footnote The nucleophile adds to the carbonyl carbon then a leaving group is eliminated.
36
Why is the **carbonyl carbon in acyl chlorides** susceptible to **nucleophilic attack**?
Partial positive charge ## Footnote The electronegative oxygen withdraws electron density from the carbonyl carbon.
37
What **product** forms when a **secondary amine reacts further with a halogenoalkane**?
Tertiary amine
38
What **product** forms when a **tertiary amine reacts further with a halogenoalkane**?
Quaternary ammonium salt
39
What is the functional group of a **secondary amine**?
–NHR ## Footnote Two alkyl groups bonded to the nitrogen and one hydrogen bonded.
40
What is the functional group of a **tertiary amine**?
NR₂ ## Footnote Three alkyl groups attached to the nitrogen.
41
What is the functional group of a **quaternary ammonium salt**?
–NR₄⁺ ## Footnote Four alkyl or aryl groups attached to nitrogen, carrying a positive charge, usually paired with a counterion like Cl⁻.
42
What type of **organic compound** contains both an **amine group** and a **carboxylic acid group**?
Amino acid ## Footnote Amino acids contain –NH₂ and –COOH functional groups.
43
Why do amino acids show both **acidic and basic behaviour**?
Two functional groups: * a basic amine group (–NH₂) * an acidic carboxyl group (–COOH) ## Footnote This dual functionality allows amino acids to act as both acids and bases, contributing to their role in biological systems.
44
# Fill in the blank: A molecule containing **both positive and negative charges** is called a _\_\_\_\_\_.
zwitterion ## Footnote Amino acids commonly exist in this form in solution.
45
# True or False: In a **zwitterion**, the amino group is protonated and the carboxyl group is deprotonated.
True ## Footnote The structure contains –NH₃⁺ and –COO⁻ groups.
46
What form does an amino acid mainly exist in at neutral pH?
Zwitterion ## Footnote The molecule has both positive and negative charges but overall neutrality.
47
# True or False: In acidic solution, the **carboxyl group** of an amino acid exists as –COO⁻.
False ## Footnote In acidic conditions it becomes –COOH.
48
# Fill in the blank: In acidic solution, the amino group of an amino acid exists as _\_\_\_\_\_.
–NH₃⁺ ## Footnote The nitrogen atom becomes protonated.
49
What happens to the **carboxyl group** of an amino acid in **alkaline solution**?
Deprotonated ## Footnote It exists as the carboxylate ion –COO⁻.
50
# True or False: In alkaline solution, the **amino group** of an amino acid exists mainly as –NH₂.
True ## Footnote The proton is removed under basic conditions.
51
# Fill in the blank: In alkaline conditions, **amino acids** form ions containing _\_\_\_\_\_ and –NH₂ groups.
–COO⁻ ## Footnote The molecule becomes negatively charged overall.
52
Why are amino acids described as **amphoteric**?
React with acids and bases ## Footnote They can donate or accept protons.
53
What property allows amino acids to form **zwitterions**?
Internal proton transfer ## Footnote The –COOH group donates H⁺ to the –NH₂ group.
54
What type of **biological macromolecules** are formed from **amino acids** joined together?
Proteins ## Footnote Proteins are long chains of amino acids linked by peptide bonds.
55
What type of **bond** links amino acids together in proteins?
Peptide bond ## Footnote A peptide bond forms between the –COOH of one amino acid and –NH₂ of another.
56
# Fill in the blank: The **linkage** formed between amino acids in proteins is called a _\_\_\_\_\_ bond.
peptide ## Footnote This bond forms through a condensation reaction.
57
# True or False: Formation of a **peptide bond** involves the removal of a molecule of water.
True ## Footnote It is a condensation reaction between the carboxyl and amine groups.
58
What level of **protein structure** refers to the sequence of amino acids in the chain?
Primary structure ## Footnote This is determined by the order of amino acids in the polypeptide.
59
# True or False: The **α-helix** and **β-pleated sheet** are examples of secondary protein structure.
True ## Footnote These structures arise from hydrogen bonding in the backbone.
60
# Fill in the blank: Hydrogen bonding stabilises the _\_\_\_\_\_ structure of proteins.
secondary ## Footnote These bonds form between the C=O and N–H groups in the chain.
61
What type of **bond** can form between sulfur atoms in certain amino acids?
Disulfide bond ## Footnote These S–S bonds help stabilise protein structure.
62
# True or False: **Disulfide** bonds help maintain the **tertiary structure** of proteins.
True ## Footnote They form cross-links within the folded protein molecule.
63
# Fill in the blank: The **three-dimensional folding** of a protein molecule is called its _\_\_\_\_\_ structure.
tertiary ## Footnote This structure results from interactions between side chains.
64
What **process** breaks peptide bonds to release individual amino acids?
Hydrolysis ## Footnote Water reacts with the peptide bond to split it.
65
What chromatographic **technique** is used to separate amino acids in the laboratory?
Thin-layer chromatography ## Footnote Amino acids are identified using their Rf values.
66
What type of **biological molecules** act as catalysts in living organisms?
Enzymes ## Footnote Enzymes speed up biochemical reactions without being used up.
67
What type of **macromolecules** are enzymes made from?
Proteins ## Footnote Their structure is formed from folded polypeptide chains.
68
# Fill in the blank: The **region** of an enzyme where the **substrate binds** is called the _\_\_\_\_\_ site.
active ## Footnote This site has a specific shape complementary to the substrate.
69
# True or False: Enzymes act as **biological catalysts**.
True ## Footnote They increase reaction rate by lowering activation energy.
70
What molecule binds to the **active site** of an enzyme during a reaction?
Substrate ## Footnote The substrate fits into the enzyme’s active site.
71
# True or False: Enzyme active sites are **stereospecific**.
True ## Footnote They can only bind molecules with the correct three-dimensional shape.
72
# Fill in the blank: Enzymes are able to recognise specific molecules due to the _\_\_\_\_\_ of the **active site**.
shape ## Footnote The active site is complementary to the substrate.
73
Why can an enzyme bind only one **enantiomer** of a molecule?
Enzyme's active site is **stereospecific**. ## Footnote Only one mirror-image form fits the active site correctly.
74
# True or False: Enzyme inhibitors work by blocking the **active site** of an enzyme.
True ## Footnote This prevents the substrate from binding.
75
# Fill in the blank: A drug that prevents **substrate binding** by occupying the active site acts as an enzyme _\_\_\_\_\_.
inhibitor ## Footnote It reduces or stops enzyme activity.
76
What concept describes the matching **shapes** of enzyme active sites and substrates?
Lock-and-key model ## Footnote The substrate fits precisely into the active site.
77
How can computers assist in **modern drug development** targeting enzymes?
Molecular modelling ## Footnote Computer simulations help design molecules that fit enzyme active sites.
78
What large **biological molecule** carries **genetic information** in living organisms?
DNA ## Footnote DNA stands for deoxyribonucleic acid.
79
What are the **repeating units** that make up **DNA** called?
Nucleotides ## Footnote DNA is a polymer formed from many nucleotide monomers.
80
# Fill in the blank: Each **nucleotide** contains a phosphate group, a pentose sugar and a _\_\_\_\_\_.
base ## Footnote The base can be adenine, thymine, cytosine or guanine.
81
# True or False: The sugar present in DNA nucleotides is **2-deoxyribose**.
True ## Footnote It is a five-carbon sugar lacking one oxygen atom compared with ribose.
82
What are the **four nitrogen-containing bases** found in DNA?
* Adenine * Cytosine * Guanine * Thymine ## Footnote These bases attach to the sugar component of the nucleotide.
83
# True or False: DNA consists of a **single long chain** of nucleotides only.
False ## Footnote DNA forms two complementary strands.
84
# Fill in the blank: The **backbone of a DNA** strand consists of alternating _\_\_\_\_\_ and sugar units.
phosphate ## Footnote These form the sugar–phosphate backbone of the molecule.
85
What **shape** is formed when two DNA strands wind around each other?
Double helix ## Footnote The two strands twist together in a helical structure.
86
# True or False: **Hydrogen bonds** hold the **two strands of DNA** together.
True ## Footnote These bonds form between complementary bases.
87
# Fill in the blank: Adenine pairs with _\_\_\_\_\_ in DNA.
thymine ## Footnote These bases are connected by hydrogen bonds.
88
Which base pairs with **guanine** in DNA?
Cytosine ## Footnote G–C pairs are also held together by hydrogen bonds.
89
Why are the two strands of DNA described as **complementary**?
Specific base pairing ## Footnote Each base forms hydrogen bonds with only one specific partner.
90
What **platinum(II) complex** is commonly used as an anticancer drug?
Cisplatin ## Footnote Cisplatin contains Pt(II) coordinated to two chloride and two ammonia ligands in a cis configuration.
91
How does cisplatin interfere with cancer cell **DNA**?
Ligand replacement with guanine ## Footnote Cisplatin forms covalent bonds between platinum and nitrogen atoms on guanine bases.
92
# Fill in the blanks: By binding to DNA, cisplatin prevents _\_\_\_\_\_ _\_\_\_\_\_ of cancer cells.
DNA replication ## Footnote Cross-links distort the DNA structure, stopping replication.
93
# True or False: Cisplatin forms bonds with **adenine** in DNA to inhibit replication.
False ## Footnote Cisplatin primarily binds to guanine nitrogen atoms.
94
What type of **chemical reaction** occurs between cisplatin and DNA?
Ligand substitution ## Footnote Chloride ligands are replaced by nitrogen atoms in DNA.
95
# True or False: The **cis configuration** of cisplatin is important for its activity.
True ## Footnote The cis arrangement allows cross-linking of adjacent guanine bases.
96
# Fill in the blank: Drugs like **cisplatin** can have adverse effects because they also affect _\_\_\_\_\_ cells.
healthy ## Footnote Rapidly dividing normal cells can be damaged, causing side effects.
97
Why must the benefits and risks of **cisplatin** be carefully assessed?
Balance of therapeutic effect vs toxicity. ## Footnote It can kill cancer cells but also harm normal cells.
98
# True or False: Cisplatin is selective only for **cancer cells** and does not affect normal cells.
False ## Footnote Some normal rapidly dividing cells are also affected.
99
# Fill in the blank: **Cisplatin** prevents DNA replication by forming covalent cross-links between _\_\_\_\_\_ bases on DNA.
guanine ## Footnote Cross-linking distorts the double helix and blocks replication.
100
What is the **primary target of cisplatin** inside a cell?
DNA ## Footnote Binding to guanine bases disrupts replication and transcription.
101
Why does **cisplatin** cause side effects such as nausea and kidney damage?
Non-specific toxicity ## Footnote Healthy cells that divide rapidly or process the drug can be affected.
102
How can you visualise **amino acids** on a **TLC plate**?
Spray with ninhydrin or view under UV light.