Lysine, $\text{H}_2\text{N}(\text{CH}_2)_4\text{CH}(\text{NH}_2)\text{COOH}$, is _______. (Note: one or more of the following options may be correct.) (i) $\alpha$-Amino acid (ii) Basic amino acid (iii) Amino acid synthesised in the body (iv) $\beta$-Amino acid

Lysine, H₂N(CH₂)₄CH(NH₂)COOH, is ____. (Note: one or more of the following options may be correct.) (i) α-Amin

NCERT Exemplar · Q58

\text{H}_2\text{N}(\text{CH}_2)_4\text{CH}(\text{NH}_2)\text{COOH}

(i)

\alpha

-Amino acid

(ii) Basic amino acid

(iii) Amino acid synthesised in the body

(iv)

\beta

-Amino acid

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Concept understanding — Amino Acid Classification

Amino Acid Classification: From Intuition to Precision

Imagine you're building with LEGO blocks. You have many different pieces — some are long, some are short, some have bumps on the side, some are flat. But all of them have one thing in common: they all click onto the same base plate. That's exactly what amino acids are like. They are the building blocks of proteins, and every single one of them shares a common "base plate" — a core structure — but differs in a side chain that gives each its unique personality.

The Common Core: What Every Amino Acid Shares

Every amino acid has a central carbon atom (called the $\alpha$ -carbon) bonded to four groups:

An amino group ( $-NH_2$ )
A carboxyl group ( $-COOH$ )
A hydrogen atom ( $-H$ )
A variable side chain (called the R group)

The R group is what makes each of the 20 standard amino acids different. It's like the unique shape and colour of each LEGO piece. The classification of amino acids is really just a way of grouping them based on what their R groups are like.

The Big Picture: Why Classify?

You classify things to understand their behaviour. In a crowded room, you might group people by height, or by what they're wearing. Similarly, amino acids are classified to predict how they will behave in water, how they interact with each other, and what role they play in a protein's structure. The most fundamental classification is based on polarity — essentially, how the R group interacts with water.

The Five Major Classes (with Intuition)

1. Nonpolar (Hydrophobic) Amino Acids

Intuition: These R groups are like oil. They hate water. They prefer to hide inside a protein, away from the watery environment of the cell.

What they look like: Their R groups are made mostly of carbon and hydrogen — no charged or polar groups. They are "greasy."

Examples: Glycine (the smallest, just a hydrogen), Alanine, Valine, Leucine, Isoleucine, Methionine, Proline (has a ring that connects back to the amino group), Phenylalanine, Tryptophan.

Note

Proline is unique — its R group forms a ring that includes the amino nitrogen, making it rigid and often causing "kinks" in protein chains.

2. Polar, Uncharged Amino Acids

Intuition: These R groups are like sugar. They dissolve in water but carry no net electric charge. They are "friendly" with water but don't have a full positive or negative charge.

What they look like: Their R groups contain oxygen, nitrogen, or sulfur atoms that can form hydrogen bonds with water.

Examples: Serine, Threonine, Cysteine (has a sulfur atom that can form disulfide bonds), Asparagine, Glutamine.

Watch out

Cysteine is often grouped here, but its sulfur atom can form a special covalent bond (disulfide bridge) with another cysteine. This is a strong, permanent link — not a weak interaction like hydrogen bonds.

3. Positively Charged (Basic) Amino Acids

Intuition: These R groups carry a positive charge at physiological pH (around 7.4). They are like magnets with a "+" sign — they attract negatively charged things.

What they look like: Their R groups contain an extra amino group ( $-NH_2$ ) that picks up a proton ( $H^+$ ) to become $-NH_3^+$ .

Examples: Lysine, Arginine, Histidine.

Important

Histidine is special — its charge changes near physiological pH. This makes it a common player in enzyme active sites where it can act as a proton donor or acceptor.

4. Negatively Charged (Acidic) Amino Acids

Intuition: These R groups carry a negative charge at physiological pH. They are like magnets with a "−" sign — they attract positively charged things.

What they look like: Their R groups contain an extra carboxyl group ( $-COOH$ ) that loses a proton to become $-COO^-$ .

Examples: Aspartic acid, Glutamic acid.

5. Aromatic Amino Acids

Intuition: These have a ring structure (a benzene ring) in their R group. They absorb ultraviolet light — a property used to measure protein concentration.

What they look like: They contain a planar, ring-shaped structure.

Examples: Phenylalanine, Tyrosine, Tryptophan.

Tip

Tyrosine and Tryptophan absorb UV light at 280 nm. This is how scientists measure protein concentration in a lab — a quick and dirty method.

--- …

Why this formula?

Amino Acid Classification: Why the Groupings Make Sense

Amino acids are the building blocks of proteins, and their classification isn't arbitrary — it's based on the chemical properties of their side chains (R-groups). Understanding why these groups behave as they do is key to mastering biochemistry for exams.

The Core Idea: The R-Group Dictates Everything

Every amino acid has a common backbone:

Amino group ( $\text{NH}_2$ )
Carboxyl group ( $\text{COOH}$ )
Hydrogen atom ( $\text{H}$ )
Variable side chain ( $\text{R}$ )

The R-group determines:

Polarity
Charge at physiological pH (~7.4)
Hydrogen bonding ability
Hydrophobicity/hydrophilicity

The Five Major Classes (and Why They Exist)

1. Nonpolar, Aliphatic (Hydrophobic) R-Groups

Examples: Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline

Why they're nonpolar:

The R-group consists of only carbon and hydrogen (hydrocarbon chains).
Carbon and hydrogen have similar electronegativity ( $\chi_C \approx 2.55$ , $\chi_H \approx 2.20$ ), so no significant dipole forms.
Water is polar; "like dissolves like" — these side chains avoid water and cluster in protein interiors.

Key exam point: Methionine has a sulfur atom, but the $\text{CH}_3\text{SCH}_2\text{CH}_2-$ group is still nonpolar because the C–S bond is nearly nonpolar.

2. Aromatic R-Groups

Examples: Phenylalanine, Tyrosine, Tryptophan

Why they're special:

Contain benzene rings (conjugated $\pi$ systems).
The delocalized electrons make them planar and rigid.
Phenylalanine is purely hydrophobic (no polar groups on ring).
Tyrosine has an –OH group → can form hydrogen bonds (partially polar).
Tryptophan has an indole ring with a nitrogen — can donate H-bonds.

Why they absorb UV light: The conjugated $\pi$ system has a small HOMO-LUMO gap, absorbing at ~280 nm — used to measure protein concentration.

3. Polar, Uncharged R-Groups

Examples: Serine, Threonine, Cysteine, Asparagine, Glutamine

Why they're polar but uncharged:

Contain electronegative atoms (O, N, S) that create partial charges.
Serine/Threonine: –OH group can donate and accept hydrogen bonds.
Cysteine: –SH group can form disulfide bonds ( $\text{–S–S–}$ ) — critical for protein structure.
Asparagine/Glutamine: –CONH $_2$ group has both carbonyl oxygen (H-bond acceptor) and amide hydrogen (H-bond donor).

Why they're uncharged at pH 7: The –OH, –SH, and –CONH $_2$ groups do not ionize significantly at physiological pH.

4. Positively Charged (Basic) R-Groups

Examples: Lysine, Arginine, Histidine

Why they're basic (proton acceptors):

Lysine: Has an $\epsilon$ -amino group ( $\text{–CH}_2\text{CH}_2\text{CH}_2\text{CH}_2\text{NH}_2$ ). The lone pair on nitrogen accepts a proton: $\text{–NH}_2 + \text{H}^+ \rightleftharpoons \text{–NH}_3^+$ pKa ≈ 10.5 → protonated at pH 7.
Arginine: Guanidino group ( $\text{–NH–C(NH}_2\text{)=NH}$ ) is resonance-stabilized when protonated — extremely basic (pKa ≈ 12.5).
Histidine: Imidazole ring has pKa ≈ 6.0 — unique because it can be neutral or positively charged near physiological pH, making it a key catalytic residue in enzymes.

5. Negatively Charged (Acidic) R-Groups

Examples: Aspartic Acid, Glutamic Acid

Why they're acidic (proton donors):

Contain a second carboxyl group ( $\text{–COOH}$ ).
At pH 7, the carboxyl group loses its proton: $\text{–COOH} \rightleftharpoons \text{–COO}^- + \text{H}^+$ …

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Lysine is a basic, $\alpha$ -amino acid that cannot be synthesised in the human body. The correct options are (A) and (B).

Lysine is one of the 20 standard amino acids, and its structure tells you almost everything you need to know. The formula given is $\text{H}_2\text{N}(\text{CH}_2)_4\text{CH}(\text{NH}_2)\text{COOH}$ . Let’s break down what each part means and why the options fall the way they do.

The key idea: an $\alpha$ -amino acid has the amino group ( $-\text{NH}_2$ ) attached to the carbon atom next to the carboxyl group ( $-\text{COOH}$ ). That carbon is called the $\alpha$ -carbon. In lysine, the central carbon in $\text{CH}(\text{NH}_2)\text{COOH}$ is that $\alpha$ -carbon — it carries both the carboxyl and one amino group. So it’s an $\alpha$ -amino acid, not a $\beta$ -amino acid (where the amino group would be on the second carbon away).

Now, why is it basic? Because there’s a second amino group at the end of the side chain: $(\text{CH}_2)_4\text{NH}_2$ . That extra $-\text{NH}_2$ can accept a proton, making the overall molecule basic. In fact, at physiological pH, lysine carries a net positive charge — it’s one of the three basic amino acids (along with arginine and histidine).

What about synthesis? The human body cannot make lysine. It is an essential amino acid, meaning it must come from the diet. So option (C) is false.

Let’s go step by step.

Identify the $\alpha$ -carbon. The general structure of an $\alpha$ -amino acid is $\text{R}-\text{CH}(\text{NH}_2)\text{COOH}$ . In lysine, the $\text{CH}(\text{NH}_2)\text{COOH}$ part matches exactly — the amino group is on the carbon adjacent to the carboxyl. So it is an $\alpha$ -amino acid. …

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Here are the common mistakes students make on this question, along with how to avoid each.

Mistake 1: Confusing $\alpha$ -Amino vs $\beta$ -Amino Acids

The Mistake:

Students see the long carbon chain $(\text{CH}_2)_4$ and assume the amino group is far from the carboxyl group, incorrectly selecting β-amino acid (Option D) or rejecting α-amino acid (Option A).

Why it happens:

They focus on the total chain length instead of the position of the first amino group relative to the carboxyl carbon.

How to Avoid:

Always locate the carboxyl carbon first (the carbon of $-\text{COOH}$ ).
The α-carbon is the carbon immediately next to the carboxyl carbon.
In lysine, the structure is: $\text{H}_2\text{N} - \text{CH}_2 - \text{CH}_2 - \text{CH}_2 - \text{CH}_2 - \text{CH}(\text{NH}_2) - \text{COOH}$ The carbon attached to $\text{NH}_2$ and $\text{COOH}$ is the α-carbon.
Rule: If the amino group is on the α-carbon, it is an α-amino acid. The second amino group on the side chain does not change this classification.

Correct choice: (A) is correct. (D) is wrong.

Mistake 2: Misclassifying Lysine as Neutral or Acidic

The Mistake:

Students see two amino groups and one carboxyl group but forget the basicity of the side chain, marking lysine as neutral or acidic.

Why it happens:

They only count the groups without considering the pKa values or the net charge at physiological pH.

How to Avoid:

Amino acids are classified by the nature of their R-group (side chain).
Lysine’s side chain is $(\text{CH}_2)_4\text{NH}_2$ . This is a basic group (it can accept a proton).
At physiological pH (~7.4), the side chain amino group is protonated ( $-\text{NH}_3^+$ ), giving lysine a net positive charge.
Memory aid: Basic amino acids have extra nitrogen atoms in their side chains (Lysine, Arginine, Histidine).

Correct choice: (B) is correct.

Mistake 3: Assuming All Amino Acids Are Essential

The Mistake: …

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Same / Similar Concept — real previous-year questions on the same or a closely similar concept, not this exact question.

Showing the 12 most recent of 26 on this concept.

AP EAPCET 2026Set eng-2026-05-12-FN1 markMCQ
$Q. Match the following List - I (Name of the amino acid) | List - II (Description) A. Tyrosine | I. Basic amino acid B. Lysine | II. Optically inactive amino acid C. Glycine | III. Sulphur containing amino acid D. Cysteine | IV. Aromatic amino acid The correct answer is (A) A - II, B - I, C - IV, D - III (B) A - IV, B - III, C - II, D - I (C) A - IV, B - I, C - II, D - III (D) A - III, B - IV, C - I, D - II$
›Reveal solutionSolution
Tyrosine → aromatic, Lysine → basic, Glycine → optically inactive, Cysteine → sulphur-containing, giving option (C).

Concept and Intuition

Amino acids differ only in their side chains, which set their properties: an aromatic ring (tyrosine), an extra basic amino group (lysine), no chiral centre when both alpha substituents are H (glycine), and a thiol group (cysteine).

Step-by-Step Solution

Tyrosine has a p-hydroxyphenyl side chain ⇒ aromatic amino acid ⇒ IV.

Lysine has a second $-NH_2$ on its side chain ⇒ basic amino acid ⇒ I.

Glycine's alpha carbon bears two H atoms, so it is not chiral ⇒ optically inactive ⇒ II.

Cysteine has a $-CH_2-SH$ side chain ⇒ sulphur-containing ⇒ III. …
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AP EAPCET 2026Set eng-2026-05-12-AN1 markMCQ
$Q. Amino acids containing hetero aromatic ring are I. Pro II. His III. Tyr IV. Trp The correct answer is (A) I, III only (B) II, IV only (C) I, II only (D) III, IV only$
›Reveal solutionSolution
Only His (imidazole) and Trp (indole) carry an aromatic ring containing a heteroatom; Pro's ring is saturated and Tyr's ring is aromatic but carbocyclic (no heteroatom in the ring).

Concept and Intuition

"Heteroaromatic" needs both conditions at once: the ring must be aromatic (planar, cyclic, conjugated, obeying Hückel's rule) AND contain at least one heteroatom (N, O, S, …) in the ring itself.

Step-by-Step Solution

Proline (Pro): its side chain forms a pyrrolidine ring fused to the α-amino group — this ring is fully saturated, not aromatic. Excluded.

Histidine (His): side chain has an imidazole ring — a 5-membered aromatic ring with two nitrogens in the ring. Aromatic + heteroatom = heteroaromatic. Included.

Tyrosine (Tyr): side chain is a phenol ring (benzene ring with an -OH) — aromatic, but the ring itself is all carbon; the heteroatom (O) is a substituent, not a ring member. Not heteroaromatic. Excluded. …
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AP EAPCET 2026Set eng-2026-05-14-FN1 markMCQ
$H_2N-CH(R)-COOH$
›Reveal solutionSolution
Matching each amino acid to its side chain (R group) gives A-III, B-I, C-II, D-IV.

Concept and Intuition

Every standard amino acid has the general structure $H_2N-CH(R)-COOH$ , differing only in the R group. Recognizing these R groups is a matter of recalling each amino acid's characteristic side chain.

Step-by-Step Solution

Alanine: simplest amino acid after glycine, R = $-CH_3$ → matches III.

Leucine: branched aliphatic side chain, R = $-CH_2-CH(CH_3)_2$ (isobutyl) → matches I.

Serine: hydroxyl-bearing side chain, R = $-CH_2-OH$ → matches II.

Cysteine: thiol-bearing side chain, R = $-CH_2-SH$ → matches IV. …
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AP EAPCET 2026Set eng-2026-05-18-FN1 markMCQ
$-NH_2$
›Reveal solutionSolution
This tests recall of amino acid side-chain functional groups: serine carries a hydroxyl ( $-OH$ ) side group and cysteine carries a thiol ( $-SH$ ) side group, so X, Y = $-OH$ , $-SH$ .

Concept and Intuition

All standard $\alpha$ -amino acids share the $-NH_2$ and $-COOH$ groups on the $\alpha$ -carbon; what distinguishes each amino acid is its side chain (R group), which often carries an additional functional group responsible for special chemistry (H-bonding, disulfide bond formation, etc.).

Step-by-Step Solution

Serine's structure is $HOCH_2-CH(NH_2)-COOH$ : besides $-NH_2$ and $-COOH$ , its side chain is $-CH_2OH$ , i.e. it carries an extra $-OH$ (hydroxyl) group. So X = $-OH$ .

Cysteine's structure is $HSCH_2-CH(NH_2)-COOH$ : its side chain is $-CH_2SH$ , i.e. it carries an extra $-SH$ (thiol) group. So Y = $-SH$ .

Matching X, Y = $-OH$ , $-SH$ against the options identifies (B).

Common Mistakes …
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AP EAPCET 2026Set ap-2026-05-19-FN1 markMCQ
$\underline{X}$
›Reveal solutionSolution
Match each amino acid's side-chain functional group to identify the –OH-bearing set (Ser, Tyr) and the –CONH2-bearing set (Gln, Asn).

Concept and Intuition

Amino acid side chains carry many different functional groups that determine their chemical behaviour. Hydroxyl (–OH) groups appear in Serine (aliphatic –CH2OH) and Tyrosine (aromatic phenolic –OH); amide (–CONH2) groups appear in Glutamine and Asparagine, the amide derivatives of glutamic acid and aspartic acid respectively.

Step-by-Step Solution

List side chains: Lys – aminobutyl (–(CH2)4NH2, basic); Gln – –CH2CH2CONH2; Ser – –CH2OH; Cys – –CH2SH; Tyr – phenol ring with –OH; Asn – –CH2CONH2.

Amino acids with –OH: Ser (III) and Tyr (V) → this is set X. …
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AP EAPCET 2025Set eng-2025-05-24-FN1 markMCQ
$Q. The list given below contains essential amino acids that are basic (X) and also non essential amino acids that are neutral (Y). X and Y, respectively are$
a) Lysine b) Alanine c) Serine d) Arginine e) Tyrosine (A) X = b, c, e; Y = a, d (B) X = a, d; Y = b, c, e (C) X = a, c; Y = b, d, e (D) X = a, b, c; Y = d, e
›Reveal solutionSolution
This tests classification of amino acids by both essentiality and acid-base character; X (essential + basic) = lysine, arginine; Y (non-essential + neutral) = alanine, serine, tyrosine.

Concept and Intuition

Amino acids are classified along two independent axes: whether the body can synthesise them (non-essential) or must obtain them from diet (essential), and their side-chain acid-base character (acidic, basic, or neutral). A question combining both axes requires checking each amino acid against both criteria simultaneously — an amino acid could be essential yet neutral, or non-essential yet basic, so care is needed not to conflate the two classifications.

Step-by-Step Solution

Lysine (a): essential, and basic (extra amino group in side chain) → fits X.

Alanine (b): non-essential, neutral (simple methyl side chain) → fits Y.

Serine (c): non-essential, neutral (hydroxymethyl side chain) → fits Y.

Arginine (d): essential (or semi-essential, classically grouped as essential in this context), and basic (guanidino side chain) → fits X. …
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AP EAPCET 2025Set eng-2025-05-26-AN1 markMCQ
$Q. Identify the essential amino acids from the following (only = only). A) Leucine B) Tyrosine C) Cysteine D) Histidine (A) A & B only (B) B & C only (C) B & D only (D) A & D only$
›Reveal solutionSolution
Tests recall of essential vs non-essential amino acids; Leucine and Histidine are essential, Tyrosine and Cysteine are not.

Concept and Intuition

"Essential" amino acids are those the human body cannot synthesise in adequate amounts through its own metabolic pathways, so they must be obtained from the diet. "Non-essential" amino acids can be synthesised in the body, often by simple transformation of another amino acid or metabolic intermediate — for instance Tyrosine is made in the body by hydroxylation of Phenylalanine, and Cysteine is made from Methionine (via the transsulfuration pathway) and serine. Leucine, being a branched-chain amino acid, and Histidine both lack the biosynthetic machinery in humans and must be supplied externally, so they are classified essential.

Step-by-Step Solution

List the standard essential amino acids for humans: Valine, Leucine, Isoleucine, Threonine, Methionine, Phenylalanine, Tryptophan, Lysine, Histidine (mnemonic "PVT TIM HALL"). …
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AP EAPCET 2025Set eng-2025-05-26-FN1 markMCQ
$Q. Consider the following. Statement-I : Lysine, arginine are essential and basic amino acids Statement-II : Leucine, phenyl alanine are non essential and neutral amino acids. Correct answer is (A) Both statement-I and statement-II are correct (B) Both statement-I and statement-II are not correct (C) Statement-I is correct, but statement-II is not correct (D) Statement-I is not correct, but statement-II is correct$
›Reveal solutionSolution
This tests classification of amino acids as essential/non-essential and acidic/basic/neutral. The answer is (C): Statement I is correct; Statement II is wrong because leucine and phenylalanine are essential, not non-essential.

Concept and Intuition

Amino acids are classified along two independent axes: (i) essential vs non-essential — whether the human body can synthesize them internally (non-essential) or must obtain them from diet (essential); and (ii) acidic/basic/neutral — based on the side-chain functional groups (extra –COOH makes it acidic, extra –NH $_2$ /basic group makes it basic, otherwise neutral).

Step-by-Step Solution

Statement I: Lysine and arginine both carry an extra basic side-chain amino/guanidino group, making them basic amino acids, and both are classified as essential amino acids (the body cannot synthesize them in sufficient amounts and they must come from the diet). This statement is CORRECT. …
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AP EAPCET 2024Set ap-2024-05-16-AN1 markMCQ
$\mathrm{COOH}$
›Reveal solutionSolution
Tests identifying two amino acids from their Fischer projections and classifying them by

essentiality; I is leucine (essential), II is serine (non-essential).

Concept and Intuition

Essential amino acids cannot be synthesised by the human body in adequate amounts and must come

from the diet; non-essential ones can be synthesised endogenously from other metabolites.

Branched-chain amino acids (leucine, isoleucine, valine) are classic essential amino acids used

directly in muscle metabolism, while simple hydroxyl-bearing amino acids like serine are readily

made in the body (e.g. from the glycolytic intermediate 3-phosphoglycerate) and are non-essential.

Step-by-Step Solution

Structure I: side chain $\mathrm{-CH_2CH(CH_3)_2}$ (isobutyl group) on the standard amino-acid backbone — this identifies it as leucine, a branched-chain essential amino acid.

Structure II: side chain $\mathrm{-CH_2OH}$ — this identifies it as serine, whose hydroxyl …
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AP EAPCET 2024Set ap-2024-05-17-FN1 markMCQ
$\mathrm{H_2N-CH(R)-COOH}$
›Reveal solutionSolution
Only the lysine side chain is correctly given; the other three options each swap in

the side chain of a different, similarly-named amino acid.

Concept and Intuition

Amino acid side chains ("R" groups) must be memorized precisely, and this question

tests classic mix-ups between structurally-related amino acids:

Lysine (Lys): $-(\mathrm{CH_2})_4-\mathrm{NH_2}$ — a 4-carbon chain ending in a primary amine, giving it a basic side chain.

Valine (Val): $-\mathrm{CH(CH_3)_2}$ (isopropyl) — a branched 3-carbon group, NOT the isobutyl group of leucine.

Threonine (Thr): $-\mathrm{CH(OH)CH_3}$ — a secondary alcohol side chain, NOT the simple $-\mathrm{CH_2OH}$ of serine.

Aspartic acid (Asp): $-\mathrm{CH_2COOH}$ — an acidic carboxylic acid side chain, NOT the amide $-\mathrm{CH_2CONH_2}$ of asparagine (its amide derivative).

Step-by-Step Solution

Check (A): Lys — $-(\mathrm{CH_2})_4\mathrm{NH_2}$ . This matches the real lysine side chain. TRUE.

Check (B): Val — $-\mathrm{CH_2CH(CH_3)_2}$ . This is actually leucine's side chain (isobutyl, one extra $\mathrm{CH_2}$ compared to valine's isopropyl). FALSE for Val.

Check (C): Thr — $-\mathrm{CH_2OH}$ . This is actually serine's side chain; threonine has an extra methyl and is $-\mathrm{CH(OH)CH_3}$ . FALSE for Thr. …
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AP EAPCET 2024Set eng-2024-05-18-FN1 markMCQ
$_2$
›Reveal solutionSolution
Matching side chains to amino acid names and recalling which are "essential" (diet-only): the isopropyl side chain identifies Valine, an essential amino acid — option (C).

Concept and Intuition

Essential amino acids are the ones the human body cannot synthesise on its own; they must be obtained from food. The standard list (memorised in NCERT biology/biomolecules chemistry) includes Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan, Threonine, Methionine, Lysine, Histidine. Alanine, Serine, Cysteine, Glycine, etc. are non-essential (the body makes them from other metabolites).

Step-by-Step Solution

Identify each amino acid from its side chain (all four share the same $H_2N-CH(-)-COOH$ backbone):

(A) $-CH_3$ : this is Alanine — non-essential.

(B) $-CH_2OH$ : this is Serine — non-essential.

(C) $-CH(CH_3)_2$ (isopropyl): this is Valine — a branched-chain amino acid, and it is essential.

(D) $-CH_2SH$ : this is Cysteine — non-essential. …
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AP EAPCET 2024Set eng-2024-05-19-AN1 markMCQ
$\mathrm{-NH_2}$
›Reveal solutionSolution
Asparagine uniquely carries a backbone $\mathrm{-NH_2}$ and $\mathrm{-CO_2H}$ plus a side-chain amide $\mathrm{-C(=O)NH_2}$ group.

Concept and Intuition

Every $\alpha$ -amino acid has a backbone $\mathrm{-NH_2}$ and $\mathrm{-CO_2H}$ . The question is really about the side chain: which amino acid's side chain is itself an amide ( $\mathrm{-CONH_2}$ )? That is asparagine, the amide of aspartic acid.

Step-by-Step Solution

Alanine's side chain is just $\mathrm{-CH_3}$ — no extra functional groups.

Arginine's side chain is a guanidino group ( $\mathrm{-NH-C(=NH)-NH_2}$ ), not an amide.

Aspartic acid's side chain is a second $\mathrm{-CO_2H}$ (carboxylic acid), not an amide. …
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Lys	Gln	Ser	Cys	Tyr	Asn
I	II	III	IV	V	VI

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Q.Lysine, H2N(CH2)4CH(NH2)COOH\text{H}_2\text{N}(\text{CH}_2)_4\text{CH}(\text{NH}_2)\text{COOH}H2​N(CH2​)4​CH(NH2​)COOH, is _______. (Note: one or more of the following options may be correct.)

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Q.Lysine, $\text{H}_2\text{N}(\text{CH}_2)_4\text{CH}(\text{NH}_2)\text{COOH}$ , is _______. (Note: one or more of the following options may be correct.)

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