Q.What role does the molecular interaction play in a solution of alcohol and water?
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Biochemical Bonds: The Glue That Holds Life Together
Imagine you're building with LEGO bricks. Some bricks click together tightly and never come apart unless you really yank them. Others snap together lightly and can be pulled apart with a gentle tug. Some bricks don't even click — they just stick because of static cling or magnetism.
Biochemical bonds are exactly like that. They are the forces that hold atoms together inside the molecules of your body — your DNA, proteins, fats, and carbohydrates. Without these bonds, you'd literally fall apart into a pile of individual atoms.
The Core Idea
Atoms bond because being bonded is more stable (lower energy) than being alone. Think of it like this: a single atom is like a person standing alone in a cold room. Bonding is like huddling together for warmth — you lose some freedom of movement, but you gain stability.
In biochemistry, we care about four main types of bonds. They differ in strength, how they form, and what they do in living systems.
1. Covalent Bonds — The Strong, Permanent LEGO Clicks
This is the strongest bond in biology. Two atoms share electrons — like two people holding the same umbrella. Each atom contributes one or more electrons, and they both "own" the pair.
Key properties:
- Very strong (100–400 kJ/mol)
- Forms the backbone of all biomolecules
- Takes a lot of energy (or enzymes) to break
Where you find it:
- The carbon-carbon bonds in your DNA's sugar-phosphate backbone
- The peptide bonds linking amino acids into proteins
- The bonds within a glucose molecule
A single covalent bond shares 2 electrons. A double bond shares 4. Triple bonds are rare in biology but exist (e.g., in cyanide).
2. Ionic Bonds — The Static Cling of Opposites
Some atoms steal electrons from others. When that happens, one atom becomes positively charged (lost an electron) and the other becomes negatively charged (gained one). Opposite charges attract — that's an ionic bond.
Key properties:
- Moderate strength (5–100 kJ/mol in dry conditions)
- Very weak in water (because water molecules get in between)
- Easily broken by changes in pH or salt concentration
Where you find it:
- In salt bridges that help proteins fold into their correct shape
- Between the phosphate groups of DNA and positively charged proteins (histones)
Ionic bonds are often called "bonds" but in water they behave more like attractions. Don't confuse them with covalent bonds — they're much weaker in biological fluids.
3. Hydrogen Bonds — The Gentle, Reversible Magnets
This is the most important weak bond in biology. A hydrogen atom that's already covalently bonded to an electronegative atom (like oxygen or nitrogen) gets a slight positive charge. It then gets attracted to another electronegative atom nearby.
Think of it like a weak magnet — it holds things together but can be easily undone.
Key properties:
- Weak individually (5–30 kJ/mol)
- But many together can be very strong
- Easily broken by heat or changes in pH
- Directional — they only work when atoms are properly aligned
Where you find it:
- Between the two strands of DNA (this is what holds the double helix together)
- In protein folding (between amino acids in the backbone)
- Between water molecules (giving water its unique properties)
Hydrogen bonds are the reason DNA can unzip for replication. If DNA used covalent bonds between strands, it would be impossible to separate without destroying the molecule.
4. Van der Waals Interactions — The Fleeting, Accidental Touches
Even neutral atoms have temporary, uneven distributions of electrons. These create tiny, momentary charges that attract nearby atoms. It's like two people accidentally brushing shoulders in a crowd — brief, weak, but real.
Key properties:
- Extremely weak (0.5–5 kJ/mol per interaction)
- Only work when atoms are very close (within 0.3–0.4 nm)
- Add up significantly when many atoms are packed together
Where you find it:
- In the hydrophobic core of proteins (where oily amino acids pack tightly)
- Between lipid tails in cell membranes
- In enzyme-substrate binding (helps "grip" the substrate)
Putting It All Together: A Biological Example
Consider a protein in your body. It's a long chain of amino acids held together by covalent peptide bonds. That chain then folds into a specific shape. The folding is guided by:
- Hydrogen bonds between backbone atoms (forming alpha helices and beta sheets)
- Ionic bonds between charged side chains …
Why this formula?
Biochemical Bonds: Why the Key Formulas Hold
Biochemical bonds are the forces that hold atoms together in biomolecules. The key formulas come from electrostatics and quantum mechanics — not from biology itself. Let's break down the why behind the most important ones.
1. Ionic Bond Energy: Coulomb's Law
Formula:
E=rk⋅q1⋅q2
Why it holds:
- Opposite charges attract — this is a fundamental law of physics (Coulomb's law).
- In a biochemical context, consider a sodium ion (Na+) and a chloride ion (Cl−). The energy released when they come together is directly proportional to the product of their charges (q1q2) and inversely proportional to the distance (r) between them.
- The constant k accounts for the medium (water vs. vacuum). In water, the effective force is weaker because water molecules partially shield the charges — this is why ionic bonds in biology are often weaker in aqueous environments.
Key insight: The formula is not arbitrary — it's derived from the inverse-square law of electrostatics, integrated over the distance the charges move toward each other.
2. Covalent Bond Energy: The Morse Potential (Approximation)
Formula (simplified):
E=De(1−e−a(r−r0))2
Why it holds:
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Covalent bonds arise from shared electrons between atoms. The energy is not a simple inverse-square law because electrons are delocalized.
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The Morse potential is an empirical formula that captures two key observations:
- At equilibrium distance (r0): Energy is minimum (E=0 in this form).
- If atoms are pulled apart (r→∞): Energy approaches De (the bond dissociation energy).
- If atoms are pushed too close (r→0): Energy skyrockets due to Pauli repulsion (electrons can't occupy the same space).
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The exponential term e−a(r−r0) models the rapid drop in attractive force as distance increases — this comes from quantum mechanical overlap of electron clouds.
Key insight: The formula is a curve fit to quantum mechanical calculations, not a first-principles derivation. But it works because it respects the physics: attraction at long range, repulsion at short range, and a stable minimum.
3. Hydrogen Bond Energy: Dipole-Dipole Interaction
Formula (approximate):
E≈−4πϵ0r32μ1μ2⋅cosθ
Why it holds:
- A hydrogen bond (e.g., between water molecules) is not a true bond — it's a strong dipole-dipole interaction.
- The dipole moment (μ) arises because oxygen is more electronegative than hydrogen, creating partial charges (δ+ and δ−).
- The energy depends on:
- Strength of dipoles (μ1μ2)
- Distance (r) — falls off as 1/r3, much faster than ionic bonds (1/r)
- Orientation (cosθ) — strongest when dipoles are aligned head-to-tail
Key insight: The 1/r3 dependence comes from the derivative of the dipole field. Unlike point charges, dipoles have a field that decays faster — this is why hydrogen bonds are directional and weaker than covalent bonds.
4. Van der Waals Interaction: Lennard-Jones Potential
Formula:
E=4ϵ[(rσ)12−(rσ)6]
Why it holds:
- Van der Waals forces arise from temporary fluctuations in electron distribution — even nonpolar molecules have instantaneous dipoles. …
In pure alcohol and in pure water the molecules are held to one another by strong hydrogen bonds (O–H⋯O). When the two liquids are mixed, alcohol–water hydrogen bonds form as well, but these new bonds are weaker than the original alcohol–alcohol and water–water hydrogen bonds.
Because the molecules in the mixture are held less tightly than in the pure liquids, their tendency to escape into the vapour increases. The vapour pressure of the solution therefore rises above the value predicted by Raoult's law, so a solution of alcohol and water shows a positive deviation from Raoult's law. …
Alcohol–water hydrogen bonds are weaker than the alcohol–alcohol and water–water bonds in the pure liquids, so molecules escape more easily, vapour pressure rises, and the mixture shows a positive deviation from Raoult's law.
Step 1 — Bonding in the pure liquids.
Both water and alcohol (ethanol) carry an O–H group, so molecules of each pure liquid are held together by strong hydrogen bonds, written as O–H⋯O. These bonds hold the molecules tightly and keep the escaping tendency (and hence the vapour pressure) of each pure liquid low.
Step 2 — What happens on mixing.
When alcohol and water are mixed, the original alcohol–alcohol and water–water contacts are partly replaced by new alcohol–water contacts. Alcohol and water molecules do form hydrogen bonds with each other, but these alcohol–water hydrogen bonds are weaker than the hydrogen bonds that existed in the two pure liquids.
Step 3 — Effect on escaping tendency.
Because the molecules in the mixture are, on average, held less tightly than in the pure liquids, they can leave the liquid surface more easily. The escaping tendency of both components rises above what it was in the pure state.
Step 4 — Effect on vapour pressure and Raoult's law. …
Method: Intermolecular Forces Analysis (Hydrogen-Bond Disruption)
This method uses the concept of hydrogen bonding to explain the behaviour of alcohol-water mixtures.
Step 1: Identify the pure components
- Water (H2O): molecules are held together by a strong, extensive hydrogen-bond network (O–H⋯O).
- Ethanol (C2H5OH): also hydrogen-bonded through its –OH group (though less extensively than water, because of the non-polar ethyl group).
Step 2: Recognise what strong H-bonding means for each pure liquid
In each pure liquid, the molecules are held tightly by their own hydrogen bonds, so their tendency to escape into the vapour — and hence the vapour pressure — is comparatively low.
Step 3: Analyse the mixture
When alcohol and water are mixed:
- Some of the original water–water and alcohol–alcohol hydrogen bonds are broken.
- New alcohol–water hydrogen bonds form in their place — but these new cross (A–B) hydrogen bonds are weaker than the alcohol–alcohol and water–water (A–A / B–B) bonds they replace.
Step 4: Identify the key molecular interaction
The dominant interaction is hydrogen bonding between the –OH group of alcohol and water molecules — and the crucial point is that, on average, this bonding in the mixture is weaker than the bonding in the pure liquids.
Step 5: State the observable consequence
- The molecules are held less tightly, so their escaping tendency increases.
- Each component exerts a higher vapour pressure than Raoult's law predicts. …
Common Mistakes: Molecular Interactions in Alcohol-Water Solutions
Mistake 1: Thinking "Like Dissolves Like" is the Only Rule
The error: Students often stop at "both are polar, so they mix" — missing the deeper mechanism.
Why it's wrong: Polarity alone doesn't explain why alcohol and water mix so readily, nor what mixing does to the vapour pressure.
How to avoid: Always ask which specific intermolecular force is at play. For alcohol-water, the key is hydrogen bonding — the -OH group in alcohol forms H-bonds with water molecules.
Key fact: Ethanol and water mix in all proportions because the -OH group of alcohol can both donate and accept hydrogen bonds with water.
Mistake 2: Ignoring the Role of the Hydrocarbon "Tail"
The error: Students think the entire alcohol molecule participates equally in H-bonding.
Why it's wrong: Only the -OH (hydroxyl) group forms H-bonds. The hydrocarbon chain (CH3CH2− in ethanol) is nonpolar and disrupts water's structure.
How to avoid: Visualize the molecule:
- Polar head (-OH) → interacts with water via H-bonds
- Nonpolar tail (alkyl group) → cannot H-bond, and gets in the way of water's own network
This is why:
- Methanol (1 carbon) mixes perfectly
- Ethanol (2 carbons) mixes perfectly
- Higher alcohols (butanol, pentanol) become less soluble — the tail dominates
Mistake 3: Assuming Mixing Must Be Exothermic Because "They Like Each Other"
The error: Students assume that since alcohol and water mix spontaneously, the mixing must release heat.
Why it's wrong: For alcohol-water, ΔHmix is slightly positive (endothermic) — the strong water-water and alcohol-alcohol H-bonds that are broken cost more energy than the weaker alcohol-water H-bonds return.
How to avoid: Remember the thermodynamic equation:
ΔGmix=ΔHmix−TΔSmix
- ΔHmix>0 (slightly endothermic — the H-bonds formed are weaker than the ones broken)
- ΔSmix>0 (large increase in entropy — molecules spread out)
- Result: ΔGmix<0 → spontaneous because entropy wins
Exam tip: For alcohol-water, entropy drives mixing, not enthalpy.
Mistake 4: Claiming Negative Deviation (Volume Contraction, Heat Release) for Alcohol-Water
The error: Students reason "new hydrogen bonds form between alcohol and water, so the molecules are held more tightly" — and conclude negative deviation from Raoult's law, with volume contraction and heat release.
Why it's wrong: The alcohol-water hydrogen bonds that form are weaker than the water-water and alcohol-alcohol hydrogen bonds they replace. The net effect of mixing is weaker average attraction, not stronger. That is why the expected answer for this NCERT question is a positive deviation from Raoult's law: the escaping tendency rises, the vapour pressure is higher than the ideal value, mixing is slightly endothermic (ΔHmix>0) and the volume slightly increases (ΔVmix>0).
How to avoid: Tie the sign of the deviation to ONE comparison — the A–B interaction versus the A–A/B–B interactions:
- A–B weaker than A–A/B–B → positive deviation (alcohol + water) …
Showing the 12 most recent of 17 on this concept.
- CBSE 2026Set 56/2/11 markMCQQ.Proteins are polymers of α-amino acids which are joined to each other by : (A) Covalent Bond (B) Peptide Bond (C) Glycosidic Bond (D) Coordinate Bond
›Reveal solutionSolution
Proteins are linear chains of α-amino acids linked by peptide bonds — a specific type of covalent bond formed between the carboxyl group of one amino acid and the amino group of the next, with the elimination of water. The correct answer is (B) Peptide Bond.
Why This Question Tests a Core Biochemical Idea
The question is about the primary structure of proteins — the simplest level of protein organization. A protein is a polymer, and like any polymer, it has repeating units (monomers) held together by a specific chemical linkage. The monomers here are α-amino acids, and the linkage that joins them is not just any covalent bond — it has a special name because of how it forms and its unique properties.
Many students get confused because all the options are types of bonds found in biomolecules. The trick is to match the bond to the specific monomers and the reaction that creates it.
Step-by-Step Reasoning
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Identify the monomers. Proteins are built from α-amino acids. Each amino acid has a central carbon (α-carbon) bonded to an amino group (−NH2), a carboxyl group (−COOH), a hydrogen atom, and a variable side chain (R). The key functional groups for linking are the −NH2 and −COOH groups.
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Understand how two amino acids join. When two amino acids link, the carboxyl group of the first amino acid reacts with the amino group of the second. This is a condensation reaction (also called dehydration synthesis) — a molecule of water (H2O) is removed. The oxygen from the carboxyl group and two hydrogens from the amino group form the water.
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Name the resulting bond. The chemical bond that forms between the carbon of the first amino acid's carboxyl group and the nitrogen of the second amino acid's amino group is called an amide bond. In biochemistry, this specific amide bond between amino acids is universally known as a peptide bond. The structure is −CO−NH−.
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Eliminate the other options.
- (A) Covalent Bond — This is too broad. A peptide bond is a covalent bond, but the question asks for the specific name of the bond joining amino acids in proteins. "Covalent bond" is the general category, not the precise answer.
- (C) Glycosidic Bond — This bond joins monosaccharides to form carbohydrates (e.g., starch, cellulose). It involves a sugar's anomeric carbon and an alcohol or another sugar. It has nothing to do with amino acids.
- (D) Coordinate Bond — This is a special type of covalent bond where both shared electrons come from the same atom. It is found in coordination complexes (e.g., metal ions with ligands) and is not the standard linkage in protein backbones. …
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- CBSE 2025Set A1 markQ.Fill in the blank: If third amino acid combines to a dipeptide, the product is called a ______.
›Reveal solutionSolution
A peptide is named by how many amino acid residues it contains: two = dipeptide, three = tripeptide, and so on.
When two amino acids join through a peptide (amide) bond, formed by condensation between the –COOH of one amino acid and the –NH2 of another (with loss of a water molecule), the product is a dipeptide. If a third amino acid molecule now condenses onto this dipeptide (forming another peptide bond), the r …
- CBSE 2024Set ANNUAL1 markQ.Name the linkage between two monosaccharide units in a disaccharide.
›Reveal solutionSolution
Two monosaccharide units are joined together by a glycosidic linkage, formed between the anomeric carbon of one sugar and a hydroxyl group of the other, with loss of a water molecule.
When two monosaccharides combine, an -OH group of one monosaccharide unit condenses with an -OH group of the anomeric carbon of the other unit, eliminating a molecule of water and forming a C–O–C bridge. This bridging oxygen linkage is called a glycosidic linkage.
…
- CBSE 2024Set ANNUAL1 markQ.What do you mean by glycosidic linkage?
›Reveal solutionSolution
A glycosidic linkage is the acetal-type C–O–C bond formed when the anomeric −OH of one sugar condenses with an −OH of another molecule, releasing water; it is the bond that links monosaccharides into disaccharides and polysaccharides.
When two monosaccharide molecules combine, the anomeric carbon (the carbon bearing the hemiacetal −OH, formed from the original aldehyde/ketone carbon) of one sugar reacts with a hydroxyl group of the second sugar. A molecule of water is eliminated, and a new C–O–C bond is formed between the two sugar rings — this bond is called a glycosidic linkage:
Sugar1−OH+HO−Sugar2⟶Sugar1−O−Sugar2+H2O …
- CBSE 2023Set ANNUAL1 markMCQQ.Proteins are polymers of amino acids, that are connected to each other by(a) glycosidic linkage(b) phosphodiester linkage(c) peptide bond(d) none of these
›Reveal solutionSolution
Proteins are condensation polymers of amino acids joined by peptide (amide) linkages.
A peptide bond forms when the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another, releasing a water molecule and forming an amide linkage (-CO-NH-). Chains of amino acids linked this way are called polypeptides, and proteins are (typically large) po …
- CBSE 2023Set ANNUAL1 markMCQQ.The linkage which holds various amino acid units in the primary structure of protein is(a) glycosidic linkage(b) hydrogen bond(c) peptide linkage(d) ionic bond
›Reveal solutionSolution
The primary structure of a protein is the linear sequence of amino acids joined by peptide (amide, −CO−NH−) bonds; the other bond types listed stabilize higher-order structure, not the primary sequence.
Peptide linkage: A peptide (amide) bond forms when the carboxyl group (−COOH) of one α-amino acid condenses with the amino group (−NH2) of another, eliminating a molecule of water:
R-CH(NH2)-COOH+H2N-CH(R’)-COOH→R-CH(NH2)-CO-NH-CH(R’)-COOH+H2O
Repeating this condensation along a chain of amino-acid residues builds a polypeptide; the specific, covalently fixed sequence of residues linked this way is the primary structure of the protein.
…
- CBSE 2022Set ANNUAL1 markMCQQ.Identify the peptide bond among the following:(a) –C(–)(–)–O–C(–)(–)– (a chain where two carbon atoms, each carrying two additional vertical bonds, are linked through a bridging oxygen)(b) –O–P(=O)(–O–)–O–C(–)(H)– (a phosphorus atom double-bonded to one O above and singly bonded to another O below, flanked by –O– and –C(H)– groups — a phosphodiester-type linkage)(c) –CO–NH–(d) –COO–
›Reveal solutionSolution
The peptide bond is the amide linkage -CO-NH-, formed between the -COOH group of one amino acid and the -NH2 group of the next, with loss of water.
Proteins are polymers of alpha-amino acids joined together by peptide bonds. A peptide bond forms when the carboxyl (-COOH) group of one amino acid condenses with the amino (-NH2) group of the next amino acid, eliminating a molecule of water:
-COOH + H2N- -> -CO-NH- + H2O
…
- CBSE 2022Set TERM21 markQ.In proteins α-amino acids are linked to each other by ................. linkage.
›Reveal solutionSolution
Amino acids join into proteins through peptide bonds, formed by condensation between the -COOH of one amino acid and the -NH2 of the next.
Proteins are polymers of α-amino acids. Two amino acids combine with the loss of a water molecule, forming an amide (-CO-NH-) bond between the carboxyl group of one amino acid and the amino group of the next:
H2N−CHR−COOH+H2N−CHR′−COOH→H2N−CHR−CO−NH−CHR′−COOH+H2O
…
- CBSE 2022Set ANNUAL1 markQ.Write the name of monomer of polymer, Nylon-6.
›Reveal solutionSolution
Nylon-6 is obtained from one monomer, caprolactam.
Nylon-6 is a synthetic condensation (step-growth) polymer of the polyamide family. It is prepared by heating caprolactam (a cyclic amide with a 6-membered ring, epsilon-caprolactam) with a trace of water, which opens the ring and polymerises it.
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- CBSE 2021Set NC1 markQ.Glycylalanine (Gly-Ala) forms by the following reaction: H2N–CH2–COOH (Glycine) +H2N–CH(CH3)–COOH (Alanine) −H2OH2N–CH2–CO–NH–CH(CH3)–COOH (Gly-Ala). Name the type of linkage connecting the two different types of amino acids (Gly and Ala).
›Reveal solutionSolution
The bond joining the −COOH of one amino acid to the −NH2 of another, with loss of a water molecule, is called a peptide linkage.
When the carboxyl group (−COOH) of glycine condenses with the amino group (−NH2) of alanine, a molecule of water is eliminated and an amide-type bond (−CO–NH−) forms between the two amino-acid residues:
H2N–CH2–COOH+H2N–CH(CH3)–COOH−H2OH2N–CH2–CO–NH–CH(CH3)–COOH
…
- CBSE 2020Set 56/1/11 markMCQQ.Assertion (A) : Sucrose is a non-reducing sugar. Reason (R) : Sucrose has glycosidic linkage. (A) Both Assertion (A) and Reason (R) are correct statements, and Reason (R) is the correct explanation of the Assertion (A). (B) Both Assertion (A) and Reason (R) are correct statements, but Reason (R) is not the correct explanation of the Assertion (A). (C) Assertion (A) is correct, but Reason (R) is incorrect statement. (D) Assertion (A) is incorrect, but Reason (R) is correct statement.
›Reveal solutionSolution
Sucrose is indeed a non-reducing sugar, and it does have a glycosidic linkage — but every disaccharide has a glycosidic linkage, so (R) doesn't explain why sucrose specifically is non-reducing. The answer is (B).
Why some sugars reduce and others don't
A reducing sugar is one that can act as a reducing agent, which requires a free or potentially free anomeric carbon — the carbon involved in the hemiacetal/hemiketal group. When this carbon is free (or can open up from a cyclic form), the sugar can exist in equilibrium with its open-chain aldehyde or ketone form, which readily reduces reagents like Fehling's or Benedict's solution.
The key question: is the anomeric carbon available, or is it locked away?
What makes sucrose special
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Sucrose's structure: Sucrose is a disaccharide made of glucose (a six-membered pyranose ring) and fructose (a five-membered furanose ring). The glycosidic bond connects C1 of glucose (its anomeric carbon) to C2 of fructose (its anomeric carbon). This is an α(1→2) linkage.
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Both anomeric carbons are involved: Unlike maltose or lactose — where one monosaccharide unit retains a free anomeric carbon that can open and close — sucrose uses both anomeric carbons in the glycosidic bond. Neither glucose nor fructose unit can revert to its open-chain form.
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No free aldehyde or ketone: Without the ability to open up, sucrose cannot expose a carbonyl group. No carbonyl means no reducing behavior.
Watch outA common mistake is thinking "glycosidic linkage = non-reducing." That's false. Maltose and lactose both have glycosidic linkages (α(1→4) and β(1→4) respectively), yet they are reducing sugars because one anomeric carbon remains free.
Evaluating the Assertion and Reason
Assertion (A): "Sucrose is a non-reducing sugar."
This is correct. Sucrose does not reduce Fehling's or Benedict's reagent because both anomeric carbons are tied up in the glycosidic bond.
Reason (R): "Sucrose has glycosidic linkage." …
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- CBSE 2020Set 56/2/11 markQ.Name the linkage formed when carboxyl end of one amino acid condenses with amino end of other amino acid.
›Reveal solutionSolution
The linkage formed is a peptide bond — a covalent amide bond (−CO−NH−) created by a condensation reaction between the carboxyl group (−COOH) of one amino acid and the amino group (−NH2) of another, releasing a water molecule.
Why This Linkage Matters
Amino acids are the building blocks of proteins. Each amino acid has a central carbon bonded to an amino group (−NH2), a carboxyl group (−COOH), a hydrogen atom, and a variable side chain (R group). To build a protein, these monomers must join end-to-end in a specific, repeating pattern.
The key chemical trick is condensation (also called dehydration synthesis). When the carboxyl end of one amino acid reacts with the amino end of another, a water molecule is eliminated — the −OH from the carboxyl and one −H from the amino group combine to form H2O. What remains is a covalent bond linking the two amino acids.
This bond is not just any bond — it is an amide bond in organic chemistry terms, but in biochemistry it has a special name.
Step-by-Step Reasoning
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Identify the reacting groups.
The first amino acid contributes its carboxyl group (−COOH). The second amino acid contributes its amino group (−NH2). These are the functional groups that must interact.
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Recognize the reaction type.
This is a condensation reaction (dehydration synthesis). The carboxyl loses an −OH group, and the amino loses one −H atom. Together they form H2O, which is released.
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Write the resulting linkage.
After water is removed, the remaining atoms form a bond:
−CO−NH−
This is a carbon-nitrogen single bond where the carbon is doubly bonded to an oxygen (a carbonyl group) and singly bonded to the nitrogen. Chemically, this is an amide bond.
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Give the biochemical name.
In the context of proteins and amino acids, this specific amide bond is called a peptide bond. It is the fundamental linkage that holds amino acids together in a polypeptide chain.
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Confirm the directionality. …
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