Q.(A) Define the following term :
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Protein Structure Levels: From a String to a Working Machine
Imagine you have a long string of beads. Each bead is a different colour, and the order of colours is fixed. If you just lay that string on a table, it's a floppy, useless line. But if you could somehow make that string fold itself into a tiny, precise 3D shape — say, a key that fits a specific lock — you'd have something that actually does a job. That's exactly what a protein is.
A protein starts as a long chain of smaller units called amino acids. There are 20 different kinds, each with a unique side chain (the "colour" of the bead). The exact sequence of these amino acids is determined by your DNA. But a protein isn't just a chain — it's a chain that folds into a specific shape, and that shape determines what the protein does. If the shape is wrong, the protein can't work.
The folding happens in stages, and we call these stages the four levels of protein structure.
Level 1: Primary Structure — The Sequence
This is the simplest level: just the linear order of amino acids in the chain, linked by peptide bonds. Think of it as the sentence written in the language of proteins.
Primary structure = the sequence of amino acids from the N-terminus (start) to the C-terminus (end).
Why does this matter? Because the sequence determines everything else. Change one amino acid in a critical spot, and the entire protein can misfold. Example: sickle cell anaemia is caused by a single amino acid swap in haemoglobin — valine replaces glutamic acid at position 6. One bead out of hundreds changes colour, and the whole protein folds wrong.
Level 2: Secondary Structure — Local Folding Patterns
The chain doesn't stay straight. Hydrogen bonds form between the backbone atoms (not the side chains) of nearby amino acids. These bonds cause the chain to twist or fold into regular, repeating patterns.
Two common patterns:
- Alpha helix (α-helix): The chain coils like a spring or a spiral staircase. Hydrogen bonds form between every 4th amino acid, holding the coil tight.
- Beta sheet (β-sheet): The chain folds back and forth like a pleated fan. Hydrogen bonds form between adjacent segments, creating a flat, sheet-like structure.
Secondary structure is stabilised entirely by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another — both part of the peptide backbone. Side chains stick out and don't participate.
These patterns are local — they happen in short stretches of the chain. A single protein can have multiple α-helices and β-sheets separated by loops.
Level 3: Tertiary Structure — The Global 3D Shape
Now the whole chain folds into its final, compact, three-dimensional shape. This is where the protein becomes functional. The tertiary structure is stabilised by interactions between the side chains of amino acids that may be far apart in the sequence but come close in space.
What holds it together?
- Hydrophobic interactions: Nonpolar side chains cluster together in the protein's interior, away from water.
- Hydrogen bonds: Between polar side chains.
- Ionic bonds: Between positively and negatively charged side chains.
- Disulfide bridges: Covalent bonds between the sulfur atoms of two cysteine amino acids — these are strong and lock parts of the chain together.
- Van der Waals forces: Weak attractions between closely packed atoms.
A common mistake: thinking tertiary structure is just "more secondary structure." It's not. Secondary structure is local folding; tertiary structure is the global arrangement of the entire chain, including how helices and sheets pack together.
Level 4: Quaternary Structure — Multiple Chains Working Together
Some proteins are made of more than one polypeptide chain. Each chain is a separate subunit, and the quaternary structure describes how these subunits assemble into a functional complex. …
Why this formula?
Protein Structure Levels: Understanding the "Why" Behind the Hierarchy
Protein structure is not defined by a single formula, but by a logical hierarchy of organization. Each level builds on the previous one, and the "formulas" here are really principles of molecular interaction that explain why proteins fold the way they do.
Let's break down each level and the reasoning behind its key features.
1. Primary Structure: The Sequence "Formula"
What it is: The linear sequence of amino acids linked by peptide bonds.
Key "formula":
Protein=NH2-[Amino Acid]1-[AA]2-...-[AA]n-COOH
Why this holds:
- Peptide bond formation is a condensation reaction:
-COOH+NH2-→-CO-NH-+H2O
- This bond is rigid and planar due to resonance (partial double-bond character). This restricts rotation, which directly influences higher-order folding.
- The sequence is determined by DNA (genetic code). Every change in sequence can alter the entire structure — this is why a single mutation (e.g., sickle cell anemia: Glu → Val at position 6) can cause disease.
Exam insight: The primary structure is the only level that is covalently determined. All higher levels are non-covalent interactions.
2. Secondary Structure: Local Folding Patterns
Key patterns: α-helix and β-pleated sheet.
Why these form — the hydrogen bond "formula":
The α-helix
- Hydrogen bonds form between the carbonyl oxygen (C=O) of residue n and the amide hydrogen (N-H) of residue n+4.
- Why n+4? This spacing allows the backbone to coil into a right-handed helix with exactly 3.6 amino acids per turn.
- Reasoning: The peptide bond's planar nature forces the backbone into a specific geometry. The n+4 pattern maximizes H-bonding while minimizing steric clashes.
The β-sheet
- Hydrogen bonds form between adjacent strands (either parallel or antiparallel).
- Why not n+4? The backbone is extended (pleated), so H-bonds occur between different segments, not within the same chain.
Key formula (Ramachandran plot):
Only certain backbone dihedral angles (ϕ,ψ) are allowed:
- α-helix: ϕ≈−57∘, ψ≈−47∘
- β-sheet: ϕ≈−130∘, ψ≈+130∘
Why these angles? Steric hindrance — atoms cannot overlap. The Ramachandran plot shows the only regions where no two atoms clash.
3. Tertiary Structure: The 3D Fold
Key "formula": The hydrophobic effect drives folding.
Why this holds:
- Water molecules form a cage-like structure around nonpolar (hydrophobic) side chains. This is entropically unfavorable (water loses freedom).
- To minimize this, hydrophobic side chains cluster together in the protein's core, away from water.
- Result: The protein collapses into a compact globule, with polar/charged residues on the surface.
Supporting interactions (the "glue"):
| Interaction | Why it matters |
|---|---|
| Hydrogen bonds | Between side chains (e.g., Ser–Glu) |
| Ionic bonds | Between charged groups (e.g., Lys–Asp) |
| Van der Waals forces | Close packing of atoms |
| Disulfide bridges | Covalent S–S bonds (only in oxidizing environments) |
Why not just one formula? Tertiary structure is unique to each protein — it's the sum of all these interactions, not a single equation.
4. Quaternary Structure: Multiple Subunits
Key "formula":
Functional protein=∑i=1nSubuniti
Why this holds:
- Some proteins need multiple polypeptide chains to function (e.g., hemoglobin: α2β2). …
Part (b)Concept understanding — Glucose Cyclization
Glucose Cyclization: From a Straight Chain to a Ring
Imagine you have a long, flexible chain with a hook at one end and an eyelet at the other. If you swing that chain around, the hook can snap into the eyelet, forming a loop. That's the core idea behind glucose cyclization.
Glucose in its simplest written form is a straight chain of six carbon atoms with an aldehyde group (−CHO) at one end. But in water (like in your blood), this chain doesn't stay straight. The aldehyde group reacts with the alcohol group on the fifth carbon, forming a stable six-membered ring.
Why does this happen?
The aldehyde carbon is electrophilic (electron-poor), and the oxygen on carbon-5 has lone pairs (nucleophilic). They attack each other, forming a new bond. This creates a hemiacetal — a carbon bonded to both an −OH and an −OR group. The ring is more stable than the open chain in solution.
The open-chain form of glucose exists in equilibrium with the cyclic form, but at any given time, over 99% of glucose molecules are in the cyclic form.
The precise statement
Glucose cyclization is an intramolecular nucleophilic addition where the aldehyde group at C1 reacts with the hydroxyl group at C5, forming a six-membered pyranose ring (named after pyran, a six-membered oxygen heterocycle). This reaction creates a new chiral center at C1, giving two possible stereoisomers called anomers: α and β.
The two anomers
When the ring forms, the oxygen from C5 becomes part of the ring. The carbon that was the aldehyde (now C1) becomes a new chiral center. The −OH group at this new center can point:
- Down (relative to the ring plane) → α-D-glucose
- Up → β-D-glucose
The α and β anomers are diastereomers, not enantiomers. They differ only at the anomeric carbon (C1). In solution, they interconvert through the open-chain form — a process called mutarotation.
How to draw it (Haworth projection)
- Draw a hexagon with an oxygen atom at the top-right corner.
- Number the carbons clockwise from the oxygen: C1 is the carbon to the right of oxygen, C2 next, and so on.
- For α-D-glucose, the −OH at C1 points down (opposite to the CH2OH group at C5).
- For β-D-glucose, the −OH at C1 points up (same side as the CH2OH group). …
Why this formula?
Glucose Cyclization: Why the Ring Forms
Glucose cyclization is a classic example of an intramolecular reaction — a molecule reacting with itself. Let's build the understanding step by step.
1. The Starting Point: Open-Chain Glucose
Glucose (C6H12O6) in its open-chain form has:
- An aldehyde group (−CHO) at carbon 1 (C1)
- A hydroxyl group (−OH) at carbon 5 (C5)
The aldehyde is electrophilic (electron-deficient at the carbonyl carbon), and the hydroxyl is nucleophilic (electron-rich oxygen with lone pairs).
2. Why Cyclization Happens: Thermodynamic & Kinetic Favorability
The Key Insight
The molecule is flexible — it can bend so that the C5 hydroxyl oxygen approaches the C1 aldehyde carbon. This brings two reactive groups into close proximity.
- Entropy is favorable: One molecule becomes one ring — no loss of translational entropy (unlike two separate molecules reacting).
- Ring strain is manageable: A 5- or 6-membered ring (furanose or pyranose) has minimal angle strain (close to tetrahedral angles).
Result: The reaction is reversible but strongly favors the cyclic form — in aqueous solution, >99% of glucose exists as the ring.
3. The Reaction: Hemiacetal Formation
The nucleophilic oxygen of the C5 hydroxyl attacks the electrophilic carbonyl carbon of C1:
R-CHO+R’-OH⇌R-CH(OH)(OR’)
This is a hemiacetal — a carbon bonded to both an −OH and an −OR group.
Mechanism (simplified)
- Protonation of the carbonyl oxygen (acid-catalyzed) makes C1 more electrophilic.
- Nucleophilic attack by the C5 oxygen.
- Deprotonation yields the cyclic hemiacetal.
4. The Key Formula(e): Ring Size & Anomeric Carbon
Ring Size Determination
The ring size depends on which hydroxyl attacks:
- C5 hydroxyl → pyranose (6-membered ring: 5 carbons + 1 oxygen)
- C4 hydroxyl → furanose (5-membered ring: 4 carbons + 1 oxygen)
For D-glucose, the C5 attack is overwhelmingly favored, giving the pyranose form.
The Anomeric Carbon
The new chiral center formed at C1 is called the anomeric carbon. Two stereoisomers arise:
- α-anomer: −OH at C1 is trans to the −CH2OH group (axial in the chair conformation)
- β-anomer: −OH at C1 is cis to the −CH2OH group (equatorial in the chair conformation)
Why two forms? The attack can occur from either face of the planar carbonyl group — leading to two possible configurations at the new stereocenter.
5. The Equilibrium Constant & Mutarotation
The interconversion between α and β anomers is called mutarotation:
α-D-glucopyranose⇌open chain⇌β-D-glucopyranose
At equilibrium (in water at 20°C):
- β-D-glucopyranose: ~64%
- α-D-glucopyranose: ~36%
- Open chain: <0.1% …
Part (a)
Reducing sugar: a carbohydrate carrying a free aldehyde or keto group (a free anomeric carbon) that can reduce Tollens' or Fehling's reagent. All monosaccharides and most disaccharides (maltose, lactose) are reducing; sucrose is not.
Fibrous vs globular proteins: fibrous are long, thread-like, water-insoluble, structural (keratin, collagen); globular are spherical, water-soluble, functional (enzymes, haemoglobin). …
Part (a): a reducing sugar has a free aldehyde/keto group; fibrous proteins are insoluble structural, globular are soluble functional; a nucleotide is a nucleoside plus a phosphate. Part (b): glucose + hydroxylamine → oxime; + acetic anhydride → pentaacetate; + conc. HNO₃ → saccharic (glucaric) acid.
Part (a)
- Reducing sugar. A reducing sugar is a carbohydrate that acts as a reducing agent because it possesses a free aldehyde or keto group (a free anomeric –OH). It reduces mild oxidants such as Tollens' (Ag+) or Fehling's (Cu2+) reagent. All monosaccharides (glucose, fructose) and most disaccharides (maltose, lactose) are reducing; sucrose is non-reducing because both anomeric carbons are engaged in the glycosidic bond.
- Differences. (i) Fibrous vs globular proteins
| Feature | Fibrous | Globular |
|---|---|---|
| Shape | long, thread-like | spherical, folded |
| Solubility | insoluble in water | soluble in water |
| Function | structural (keratin, collagen, silk) | functional (enzymes, hormones, haemoglobin) |
(ii) Nucleotide vs nucleoside
| Feature | Nucleoside | Nucleotide |
|---|---|---|
| Composition | base + pentose sugar | base + pentose sugar + phosphate |
Showing the 12 most recent of 20 on this concept.
- COMEDK 2026Set 2026-A1 markMCQQ.A small segment of a polypeptide gave on complete hydrolysis 3 molecules of alanine, 2 molecules of glycine and 3 molecules of cysteine. What is the number of peptide linkages in the segment of the polypeptide? (A) 7 (B) 8 (C) 6 (D) 5
›Reveal solutionSolution
The number of peptide bonds in a polypeptide is always one less than the number of amino acid residues. Here, total residues = 3 + 2 + 3 = 8, so peptide bonds = 8 − 1 = 7. The correct option is (A).
Concept & Intuition
A polypeptide is a chain of amino acids linked by peptide bonds. Each peptide bond forms between the carboxyl group of one amino acid and the amino group of the next. If you have n amino acids in a chain, you need exactly n−1 peptide bonds to connect them — like linking n beads on a string requires n−1 knots. Hydrolysis breaks all these bonds, releasing the individual amino acids. So counting the total number of amino acids released tells you the original chain length, and subtracting one gives the number of peptide bonds.
Step-by-step reasoning
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Identify the total number of amino acid residues.
Complete hydrolysis of the polypeptide yields:
- 3 molecules of alanine
- 2 molecules of glycine
- 3 molecules of cysteine Total = 3+2+3=8 amino acid molecules.
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Relate residues to peptide bonds. …
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- COMEDK 2026Set 2026-M1 markMCQQ.The secondary structure of protein consists of: (A) A long chain of amino acids linked with each other in a specific sequence (B) A folding of the polypeptide chains which exists as fibrous and globular (C) A long polypeptide chain which exists α-helix and β-pleated sheet structure (D) Two or more polypeptide chains which exist as sub-units
›Reveal solutionSolution
The secondary structure of a protein refers to the local, regular folding patterns of the polypeptide backbone, specifically the α-helix and β-pleated sheet, not the sequence, overall shape, or subunit assembly. The correct option is (C).
The key here is to recall the hierarchy of protein structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein’s architecture. The secondary structure is the local spatial arrangement of the polypeptide backbone, stabilized mainly by hydrogen bonds between the carbonyl oxygen and amide hydrogen of amino acids that are close in sequence. It does not involve the side chains (R-groups) or the overall 3D shape of the entire chain.
Let’s examine each option:
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Option (A) describes “a long chain of amino acids linked in a specific sequence.” That is the primary structure — the linear order of amino acids held together by peptide bonds. This is not secondary structure.
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Option (B) says “a folding of the polypeptide chains which exists as fibrous and globular.” This refers to the tertiary structure (the overall 3D shape of a single polypeptide chain) or even the classification of proteins based on shape. Fibrous and globular are categories of tertiary/quaternary structure, not secondary. …
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- COMEDK 2025Set 2025-E1 markMCQQ.Two statements, one Assertion and the other Reason are given. Choose the right option. Assertion : Insulin is called a protein whereas Glycyl alanine is not called a protein Reason : A polypeptide with amino acid residue less than 100 can also be called as a protein if it has a well-defined conformation of a protein. (A) Assertion is correct but Reason is incorrect (B) Both Assertion and Reason are incorrect (C) Both Assertion and Reason are correct (D) Assertion is incorrect but Reason is correct
›Reveal solutionSolution
Both statements are correct: insulin (51 residues, well-defined conformation) qualifies as a protein even though it has fewer than 100 residues, whereas glycyl-alanine (a dipeptide) does not.
Assertion: Insulin is a protein; glycyl-alanine (a dipeptide) is not. This is true — insulin, though only 51 amino-acid residues, has a definite three-dimensional structure and biological function, so it is classed as a protein, while a simple dipeptide is not. …
- COMEDK 2025Set 2025-M1 markMCQQ.Choose the incorrect statement. (A) The hormone Glucocorticoid controls the level of excretion of water and salts by the kidney. (B) Vitamins A and K are fat soluble and are stored in the liver of human beings. (C) Denaturation of protein is due to loss of both the secondary and tertiary structures of the protein. (D) Complete hydrolysis of RNA gives Nitrogen containing bases, a pentose sugar and phosphoric acid.
›Reveal solutionSolution
The question asks for the incorrect statement. Glucocorticoids regulate metabolism and inflammation, not water/salt excretion (that’s mineralocorticoids like aldosterone). So option (A) is false; the others are true.
Concept & Intuition
This is a biology fact-checking problem. You need to recall specific functions of hormones, properties of vitamins, protein denaturation, and RNA hydrolysis. The trick is to spot the mismatch between a hormone’s actual role and the statement. Glucocorticoids (e.g., cortisol) are often confused with mineralocorticoids (e.g., aldosterone) because both come from the adrenal cortex. The key distinction: glucocorticoids handle stress, metabolism, and immune suppression; mineralocorticoids handle electrolyte and water balance.
Step-by-step reasoning
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Evaluate statement (A):
Glucocorticoids (like cortisol) primarily regulate glucose metabolism, suppress inflammation, and help the body respond to stress. They do not control water and salt excretion by the kidney. That job belongs to mineralocorticoids (e.g., aldosterone), which promote sodium retention and potassium excretion. Therefore, statement (A) is incorrect.
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Evaluate statement (B):
Vitamins A, D, E, and K are fat-soluble. Vitamin A is stored in the liver (as retinol esters), and vitamin K is also stored in the liver (though in smaller amounts). This statement is correct.
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Evaluate statement (C): …
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- KCET 2024Set B-21 markMCQQ.α–D–(+)–glucose and β–D–(+)–glucose are: (A) Enantiomers (B) Conformers (C) Epimers (D) Anomers
›Reveal solutionSolution
α- and β-D-glucose differ in configuration at exactly one carbon — C-1, the anomeric carbon created on ring closure — so by definition they are anomers.
1. Where the α/β difference comes from
Open-chain D-glucose is an aldohexose. Its C-5 –OH attacks the C-1 aldehyde carbon intramolecularly, forming a six-membered cyclic hemiacetal (the pyranose ring):
CHO (C-1, planar, sp2)⟶HCOH(C-1, sp3, a NEW stereocentre)
Because the carbonyl carbon is planar, the ring oxygen can close from either face, so the new –OH at C-1 ends up either:
- down (trans to the CH2OH; on the same side as the C-2 OH in Fischer projection) ⇒ α-D-(+)-glucose, or
- up ⇒ β-D-(+)-glucose.
The carbon whose configuration is fixed by this ring closure is called the anomeric carbon, and the two products are anomers. In solution they interconvert through the open-chain form — the phenomenon of mutarotation ([α]D drifting from +111∘ for pure α and +19∘ for pure β to the equilibrium +52.7∘).
2. Eliminate the other terms precisely
- (A) Enantiomers — non-superimposable mirror images: they must differ at every stereocentre. α- and β-D-glucose share the same configuration at C-2, C-3, C-4 and C-5, so they are not mirror images (they are diastereomers). ✗ …
- COMEDK 2024Set 2024-A1 markMCQQ.Among the following peptides, identify the pair where the name and its structure are correctly matched. (A) (B) (C) (D)
›Reveal solutionSolution
The key is to match the side‑chain sequence in the condensed structure with the standard three‑letter amino‑acid abbreviations (N‑terminal to C‑terminal). Only option (C) correctly names the tripeptide Ala‑Gly‑Phe.
Concept & Intuition
Peptide names are written from the N‑terminal (free amino end) to the C‑terminal (free carboxyl end). Each three‑letter code corresponds to a specific side chain:
- Gly (glycine): side chain = H (i.e., the α‑carbon is –CH₂–).
- Ala (alanine): side chain = –CH₃.
- Phe (phenylalanine): side chain = –CH₂C₆H₅ (benzyl).
To check correctness, read the structure from left (N‑terminus) to right (C‑terminus) and list the side chains in order. Then compare that sequence to the name.
Step‑by‑step reasoning
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Option (A):
Structure: H₂N–CH₂–C(=O)–NH–CH(–CH₂SH)–COOH
- First residue: α‑carbon has no side chain (just –CH₂–) → Gly.
- Second residue: α‑carbon has –CH₂SH (cysteine side chain) → Cys, not Ala. Name given: “Gly‑Ala” → mismatch (should be Gly‑Cys). ✗ Incorrect.
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Option (B):
Structure: H₂N–CH₂–C(=O)–NH–CH(–CH₃)–COOH
- First residue: –CH₂– → Gly.
- Second residue: –CH₃ → Ala. Name given: “Ala‑Gly” → order reversed (N‑terminal is Gly, not Ala). ✗ Incorrect.
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Option (C):
Structure: H₂N–CH(–CH₃)–C(=O)–NH–CH₂–C(=O)–NH–CH(–CH₂C₆H₅)–COOH
- First residue: –CH₃ → Ala.
- Second residue: –CH₂– (no side chain) → Gly.
- Third residue: –CH₂C₆H₅ → Phe. Name given: “Ala‑Gly‑Phe” → matches exactly. ✓ Correct.
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Option (D): …
- COMEDK 2024Set 2024-A1 markMCQQ.Which of the following statement is not true about glucose? (A) Glucose does not give Schiff's reagent test (B) Glucose on reaction with HI and red P at 373 K gives a mixture of cyclohexane and 1-iodohexane (C) Both α-D-glucose and β-D-glucose undergo mutarotation in aqueous solutions (D) Glucose reacts with hydroxylamine to form an oxime
›Reveal solutionSolution
The question asks which statement about glucose is false. By checking each option against known glucose chemistry, we find that option (B) is incorrect because the reaction with HI and red P at 373 K yields n-hexane, not a mixture of cyclohexane and 1-iodohexane.
Concept & Intuition
Glucose is an aldohexose — a six-carbon sugar with an aldehyde group (in open-chain form) and multiple hydroxyl groups. Its reactions depend on these functional groups: the aldehyde gives typical carbonyl reactions (oxime formation, no Schiff’s test because it’s usually cyclic), the hydroxyls can be reduced, and the anomeric carbon allows mutarotation. To spot the false statement, we need to recall the specific outcome of each reaction, especially the drastic reduction with HI and red phosphorus, which removes all oxygen atoms.
Step-by-step reasoning
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Option (A): Glucose does not give Schiff’s reagent test
Schiff’s reagent tests for aldehydes, but glucose exists predominantly in cyclic hemiacetal form, where the aldehyde group is masked. The equilibrium concentration of free aldehyde is too low to give a positive test under normal conditions. Thus, this statement is true.
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Option (B): Glucose on reaction with HI and red P at 373 K gives a mixture of cyclohexane and 1-iodohexane
HI and red phosphorus are a powerful reducing agent that removes all hydroxyl groups (as water) and reduces any carbonyl to methylene. For glucose (C₆H₁₂O₆), the complete reduction yields straight-chain n-hexane (C₆H₁₄). No cyclohexane forms because the carbon skeleton remains unbranched and no ring closure occurs under these conditions. Also, 1-iodohexane would be an intermediate, but excess HI and red P drive reduction all the way to the alkane. So the product is n-hexane, not a mixture of cyclohexane and 1-iodohexane. This statement is false.
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Option (C): Both α-D-glucose and β-D-glucose undergo mutarotation in aqueous solutions …
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- COMEDK 2024Set 2024-E1 markMCQQ.Given are 4 statements related to the chemical properties of Glucose. Identify the two incorrect statements from the following. A. It reacts with Br2 (aq) to form Saccharic acid. B. Reacts with Acetic anhydride to form Glucose tetraacetate. C. Reacts with Hydroxylamine to give Glucose oxime. D. It reacts with ammoniacal AgNO3 to form ammonium salt of Gluconic acid with deposition of silver. (A) A & B (B) C & D (C) B & D (D) A & C
›Reveal solutionSolution
Statements A (Br2 water → saccharic acid) and B (acetic anhydride → tetraacetate) are the incorrect ones; C and D correctly describe glucose chemistry.
A. Br2(aq) → Saccharic acid — INCORRECT. Bromine water is a mild oxidising agent; it oxidises only the –CHO group of glucose to –COOH, giving gluconic acid. Saccharic (glucaric) acid, a dicarboxylic acid, requires the stronger oxidant conc. HNO3.
B. Acetic anhydride → Glucose tetraacetate — INCORRECT. Glucose has five –OH groups, all acetylated, giving glucose pentaacetate, not tetraacetate. …
- COMEDK 2024Set 2024-M1 markMCQQ.Identify the 2 chemical tests which is not answered by Glucose having an open chain structure [A] Reaction with Schiff's reagent and with Sodium bisulphite [B] Reaction with HCN and with HI [C] Reaction with HNO3 and with Acetic anhydride [D] Reaction with aqueous Bromine and with Hydroxylamine (A) [D] (B) [B] (C) [C] (D) [A]
›Reveal solutionSolution
Glucose’s open-chain aldehyde structure explains most of its reactions, but two tests—reaction with Schiff’s reagent and with sodium bisulphite—are not given by the open-chain form because in solution glucose exists predominantly as a cyclic hemiacetal, which lacks a free aldehyde group.
The key concept here is mutarotation and the equilibrium between open-chain and cyclic forms of glucose. In water, glucose is almost entirely (over 99%) in its cyclic pyranose form. Only a tiny fraction exists as the free aldehyde. Many aldehyde-specific tests require a high enough concentration of the free aldehyde to give a visible positive result. Some tests are so sensitive that even the trace amount of open-chain form suffices; others are not.
Let’s examine each pair of tests.
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Reaction with Schiff’s reagent and with Sodium bisulphite
- Schiff’s reagent (fuchsine decolorized by SO₂) gives a magenta color with aldehydes. However, glucose gives a very slow or no color change because the equilibrium concentration of the free aldehyde is too low to react quickly.
- Sodium bisulphite (NaHSO₃) adds to aldehydes to form a crystalline bisulphite addition product. Glucose does not form such a solid adduct under normal conditions, again because the open-chain form is too scarce.
- Conclusion: These two tests are not answered by the open-chain structure in practice.
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Reaction with HCN and with HI
- HCN adds to the carbonyl group of the open-chain form to give a cyanohydrin. This reaction does occur (though slowly) because the equilibrium shifts as the open-chain form is consumed.
- HI reduces the aldehyde group (and also the alcohol groups) under drastic conditions, but the aldehyde is still the reactive site.
- Conclusion: Both are possible via the open-chain form.
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Reaction with HNO₃ and with Acetic anhydride
- HNO₃ oxidizes the aldehyde group to a carboxylic acid (giving gluconic acid) and also the terminal CH₂OH to COOH (giving glucaric acid). This clearly involves the open-chain aldehyde.
- Acetic anhydride reacts with all –OH groups (including the hemiacetal OH) to form an acetate. This does not require the open-chain form; it reacts with the cyclic form as well. So this test is not exclusive to the open-chain structure, but the question asks which tests are not answered by the open-chain structure — meaning which tests fail if only the open-chain form is considered. Acetic anhydride works fine, so it’s not a “not answered” case.
- Conclusion: HNO₃ works via the open-chain; acetic anhydride works anyway.
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Reaction with aqueous Bromine and with Hydroxylamine …
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- COMEDK 2024Set 2024-M1 markMCQQ.Given below are 4 statements about Insulin. Which of these statement/(s) is/are correct? [A] Insulin is a globular protein consisting of 51 Amino acids. [B] Insulin is constituted of 3 polypeptide chains linked together. [C] Insulin is constituted of 2 polypeptide chains linked together by disulphide bonds. [D] The 3 polypeptide chains in Insulin are linked together by Hydrogen bonding. (A) [D] (B) [A] & [C] (C) [B] & [D] (D) [B]
›Reveal solutionSolution
Insulin is a globular protein with 51 amino acids arranged in two polypeptide chains (A and B) linked by disulphide bonds, so only statements [A] and [C] are correct.
Concept and Intuition
Insulin is a classic example of a small, well-studied protein. Its structure is fundamental in biochemistry: it is synthesized as a single chain (proinsulin) that is later cleaved to remove a connecting peptide (C-peptide), leaving two chains — the A chain (21 amino acids) and the B chain (30 amino acids). These two chains are held together by disulphide bonds (covalent bonds between cysteine residues), not by hydrogen bonds between separate chains. Hydrogen bonds are important for the protein’s three-dimensional folding, but they do not link the two chains together. Knowing this, we can evaluate each statement.
Step-by-step reasoning
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Statement [A]: “Insulin is a globular protein consisting of 51 Amino acids.”
- Insulin is indeed a globular protein (soluble, roughly spherical shape). The total number of amino acids in the active form is 21 (A chain) + 30 (B chain) = 51.
- This statement is correct.
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Statement [B]: “Insulin is constituted of 3 polypeptide chains linked together.”
- Mature insulin has only two chains (A and B). The third chain (C-peptide) is present only in the precursor proinsulin and is removed during processing.
- This statement is incorrect.
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Statement [C]: “Insulin is constituted of 2 polypeptide chains linked together by disulphide bonds.”
- Exactly right: the A and B chains are connected by two interchain disulphide bonds (between A7–B7 and A20–B19). There is also one intrachain disulphide bond within the A chain (A6–A11).
- This statement is correct.
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Statement [D]: “The 3 polypeptide chains in Insulin are linked together by Hydrogen bonding.” …
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- KCET 2023Set B-41 markMCQQ.Match List-I and List-II with respect to proteins and their functions and select the correct option. List-I | List-II
- Collagen | p. Fights infectious agents
- Trypsin | q. Hormone
- Insulin | r. Enzyme
- Antibody | s. Intercellular ground substance (A) 1-s, 2-p, 3-r, 4-p (B) 1-q, 2-r, 3-q, 4-s (C) 1-s, 2-q, 3-r, 4-p (D) 1-s, 2-r, 3-q, 4-p
›Reveal solutionSolution
Assign each protein its biological role: collagen → ground substance, trypsin → enzyme, insulin → hormone, antibody → defence.
Concept — Proteins and their functions (Biomolecules). NCERT gives a table of proteins with their functions; each protein here has exactly one role.
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Collagen — the most abundant protein in the animal world; it is the fibrous protein of the intercellular ground substance of connective tissue. → s
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Trypsin — a proteolytic enzyme secreted (as trypsinogen) by the pancreas; it hydrolyses proteins in the small intestine. → r
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Insulin — a peptide hormone secreted by the β-cells of the islets of Langerhans; it lowers blood glucose. → q
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Antibody — an immunoglobulin that fights infectious agents (antigens/pathogens). → p …
- COMEDK 2023Set 2023-E1 markMCQQ.Structures of 3 Monosaccharides are given below. Two of them are Anomers. Identify the two Anomers. (A) II is the anomer of both I and II (B) I and II are Anomers. (C) II and III are Anomers. (D) I and III are Anomers
›Reveal solutionSolution
[I] and [III] differ only at the anomeric carbon C1 (identical at C2–C4), so they are anomers; [II] also differs at C2 and is not an anomer of either.
Definition: anomers are a special pair of epimers (cyclic monosaccharides) that differ in configuration only at the anomeric carbon (C1, the former carbonyl carbon).
Compare the structures at C1–C4 (left/right substituents):
- [I]: C1 = H/OH, C2 = H/OH, C3 = HO/H, C4 = H/OH
- [III]: C1 = HO/H, C2 = H/OH, C3 = HO/H, C4 = H/OH
- [II]: C1 = HO/H, C2 = HO/H, C3 = HO/H, C4 = H/OH …
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