Q.Amino acids can be classified as α-, β-, γ-, δ- and so on depending upon the relative position of the amino group with respect to the carboxyl group. Which type of amino acids forms polypeptide chain in proteins?
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🔒 Start your 14-day free trial to unlock the full solution →Concept understanding — De Broglie Wavelength
De Broglie Wavelength: When Particles Start Acting Like Waves
Imagine you're holding a cricket ball. You know exactly where it is, and if you throw it, you can predict its path. That's a particle — localised, definite, following Newton's laws. Now think of light. You can't "hold" a beam of light; it spreads out, bends around corners, creates interference patterns. That's a wave — spread out, not localised.
For centuries, physics kept these two worlds separate. Particles were particles. Waves were waves. Never the twain shall meet.
Then came a young French physicist, Louis de Broglie, in 1924. He asked a question that seemed almost absurd: If light — which we thought was a wave — can behave like a particle (the photoelectric effect), then why can't a particle — say, an electron — behave like a wave?
That question turned physics upside down.
The Core Idea
De Broglie proposed that every moving particle has a wave associated with it. The wavelength of that wave depends on the particle's momentum. The faster or heavier the particle, the shorter the wavelength.
λ=ph=mvh
Where:
- λ = de Broglie wavelength (in metres)
- h = Planck's constant (6.626×10−34 J⋅s)
- p = momentum of the particle (mv for non-relativistic speeds)
This is not a mathematical trick. It's a physical reality. An electron moving through a crystal actually behaves like a wave of this wavelength — it can diffract, interfere, and form patterns just like light does.
Why You Don't See It in Daily Life
Here's the crucial point: the de Broglie wavelength is incredibly tiny for everyday objects.
Take a cricket ball of mass 0.16 kg moving at 30 m/s. Its de Broglie wavelength is:
λ=0.16×306.626×10−34≈1.38×10−34 m
That's about a hundred trillion trillion times smaller than the nucleus of an atom. No experiment can detect such a wave — it's effectively zero for all practical purposes.
Now take an electron (mass 9.1×10−31 kg) accelerated through 100 volts. Its speed is about 5.9×106 m/s. Its de Broglie wavelength:
λ=9.1×10−31×5.9×1066.626×10−34≈1.23×10−10 m
That's about 0.12 nanometres — comparable to the spacing between atoms in a crystal. This is measurable. And indeed, in 1927, Davisson and Germer fired electrons at a nickel crystal and observed diffraction — the unmistakable signature of a wave.
The de Broglie wavelength is only observable when it is comparable to the size of objects the particle interacts with. For macroscopic objects, it's far too small to matter. For subatomic particles, it's the key to understanding their behaviour.
What This Means Physically
The wave is not a physical wave in space like a water wave. It's a probability wave — its amplitude at any point tells you the probability of finding the particle there. Where the wave amplitude is large, you're likely to find the particle; where it's zero, you won't.
This wave-particle duality is not a compromise. It's the actual nature of reality. An electron is neither a pure particle nor a pure wave — it's something that shows particle-like behaviour in some experiments (like hitting a screen at a point) and wave-like behaviour in others (like passing through two slits and interfering with itself). …
Why this formula?
De Broglie Wavelength: Why the Formula Holds
Let's build this from the ground up — understanding why matter has a wavelength, not just memorizing λ=ph.
The Core Insight: Nature's Symmetry
Before de Broglie, physics had two separate worlds:
- Light — showed wave behaviour (diffraction, interference) but also particle behaviour (photoelectric effect)
- Matter — showed particle behaviour (momentum, collisions) but no wave behaviour yet
De Broglie asked a daring question in his 1924 PhD thesis:
If light (a wave) can behave like a particle, why can't a particle (like an electron) behave like a wave?
Nature should be symmetric — what applies to one should apply to the other.
Step 1: Start with Light (What We Already Knew)
For a photon, Einstein had given us two key relations:
- Energy: E=hf (Planck's relation)
- Momentum: p=λh (from E=pc for light, combined with c=fλ)
So for light:
λ=ph
This was experimentally verified for photons.
Step 2: De Broglie's Bold Hypothesis
De Broglie said: This relation is not special to light. It is universal.
For any particle with momentum p:
λ=ph
Where:
- λ = de Broglie wavelength
- h = Planck's constant (6.626×10−34 J⋅s)
- p = momentum of the particle
Step 3: Why Momentum and Not Velocity?
This is crucial. The formula uses momentum (p=mv), not just velocity.
For a non-relativistic particle (slow compared to light):
λ=mvh
For a relativistic particle (like an electron at high speed):
p=γmvwhereγ=1−v2/c21
λ=γmvh
Why momentum? Because momentum is the more fundamental quantity — it's conserved, it's frame-independent in a deeper sense, and it connects directly to the wave's phase.
Step 4: The Deeper Reasoning — Wave-Particle Duality
De Broglie didn't just guess. He reasoned:
- Every moving particle has an associated wave — called the "matter wave" or "pilot wave"
- The frequency of this wave comes from energy: f=hE
- The wavelength comes from momentum: λ=ph
These two relations are linked by the phase velocity of the wave:
vphase=fλ=hE⋅ph=pE
For a free particle with kinetic energy E=2mp2:
vphase=2mp=2v
This is half the particle's speed — a strange but mathematically consistent result.
Step 5: Experimental Confirmation (Why We Believe It)
De Broglie's idea was confirmed when electrons showed wave behaviour: …
The key idea is that only α-amino acids — where the amino group is attached to the carbon adjacent to the carboxyl group — can form the peptide bonds that link into a polypeptide chain.
Reasoning:
- In a polypeptide chain, each amino acid is joined to the next by a peptide bond formed between the α-amino group (−NH2) of one amino acid and the α-carboxyl group (−COOH) of another. …
Only α-amino acids — those with the amino group on the carbon adjacent to the carboxyl group — form the polypeptide chains found in proteins, because their structure allows peptide bonds to link without steric hindrance.
The key to this question lies in understanding what a polypeptide chain actually is, and why nature chose a specific geometry for it.
Proteins are built from amino acids linked by peptide bonds. A peptide bond forms between the carboxyl group (−COOH) of one amino acid and the amino group (−NH2) of another. But here’s the catch: for this bond to form efficiently and for the resulting chain to fold into functional shapes, the amino and carboxyl groups must be attached to the same carbon atom — the α-carbon.
Why? Because in an α-amino acid, the amino group and the carboxyl group are separated by exactly one carbon. This places them close enough to react easily, and the resulting backbone has a regular, repeating pattern: —NH—CHR—CO—. This pattern is what allows the chain to adopt stable secondary structures like α-helices and β-sheets.
If you used a β-amino acid (amino group on the second carbon from the carboxyl), the backbone would have an extra carbon inserted, making the chain longer, more flexible, and unable to pack into the compact, stable folds required for protein function. γ-, δ-, and higher amino acids would make the backbone even more irregular.
So the answer is straightforward: only α-amino acids are used in natural protein synthesis.
A common mistake is to think that any amino acid with both groups can form a peptide bond. While technically possible in a lab, only α-amino acids produce the specific backbone geometry that living systems use for functional proteins.
The α-carbon is the central carbon in an amino acid. It’s the one that carries the amino group, the carboxyl group, a hydrogen atom, and a variable side chain (R group). If the amino group is on any other carbon, it’s not an α-amino acid.
The general structure of an α-amino acid:
H2N−CαH(R)−COOH …
Concept: Amino Acid Classification by Position of Amino Group
The classification (α, β, γ, δ, etc.) depends on which carbon atom (relative to the carboxyl carbon) the amino group (−NH2) is attached to.
- α-amino acid: Amino group on the first carbon (carbon-2, i.e., the carbon adjacent to the carboxyl group).
- β-amino acid: Amino group on the second carbon (carbon-3).
- γ-amino acid: Amino group on the third carbon (carbon-4), and so on.
Method: Structural Identification & Biological Context
Method name: Carbon-numbering rule for amino acid classification
Steps:
- Identify the carboxyl group (−COOH) — this is the reference point.
- Number the carbon chain starting from the carboxyl carbon (carbon-1).
- Locate the carbon to which the amino group (−NH2) is attached.
- Classify based on the carbon number:
- Carbon-2 → α-amino acid
- Carbon-3 → β-amino acid
- Carbon-4 → γ-amino acid
- Apply biological knowledge: Proteins (polypeptides) are built exclusively from α-amino acids.
Answer
α-amino acids form polypeptide chains in proteins.
Why only α-amino acids? …
The Core Concept
Amino acids in proteins are linked by peptide bonds to form polypeptide chains. The key point is that only α-amino acids (where the amino group is attached to the carbon adjacent to the carboxyl group) are used in natural protein synthesis.
Common Mistakes & How to Avoid Them
✗ Mistake 1: Thinking any amino acid can form a polypeptide chain
Why it happens: Students memorise that "amino acids form proteins" but forget the structural restriction.
How to avoid:
- Remember: only α-amino acids have the amino group on the α-carbon (the carbon next to the –COOH group).
- In β-, γ-, or δ-amino acids, the amino group is further away — this prevents the correct alignment needed for peptide bond formation during ribosomal translation.
Key exam point: Polypeptide chains in proteins are built exclusively from α-amino acids.
✗ Mistake 2: Confusing "polypeptide chain" with "peptide bond formation in general"
Why it happens: Some non-α amino acids can form amide bonds in lab conditions, so students assume they can form polypeptides in nature.
How to avoid:
- Distinguish between chemical peptide bond formation (possible with any amino acid in a test tube) and biological polypeptide synthesis (ribosome-based, requires α-amino acids).
- In exams, "polypeptide chain in proteins" always refers to natural, biological chains.
✗ Mistake 3: Forgetting the α-carbon definition
Why it happens: Students confuse the numbering of carbon atoms in amino acids.
How to avoid:
- Draw a generic amino acid: H2N−CHR−COOH The carbon bearing both the –NH2 and –COOH groups is the α-carbon.
- If the amino group is on the next carbon (C2 from –COOH), it's β; on C3, it's γ, and so on.
✗ Mistake 4: Assuming β- or γ-amino acids are irrelevant
Why it happens: Some textbooks mention them only briefly, so students ignore them.
How to avoid: …
- KCET 2026Set D31 markMCQQ.Which of the following represents de Broglie equation? (A) λ=mνh (B) λ=mνh (C) λ=mph (D) λ=pμ
›Reveal solutionSolution
The de Broglie relation connects a moving particle's wavelength to its momentum via Planck's constant.
Step 1 — de Broglie's hypothesis
Louis de Broglie proposed that every moving particle of mass m and velocity ν has an associated "matter wave" whose wavelength λ is inversely proportional to its momentum p=mν.
Step 2 — The equation
This gives λ=ph=mνh, where h is Planck's constant.
Step 3 — Eliminating the other options …
- KCET 2023Set A-31 markMCQQ.When light propagates through a given homogeneous medium, the velocities of (A) primary wavefronts are lesser than those of secondary wavelets. (B) primary wavefronts are greater than or equal to those of secondary wavelets. (C) primary wavefront and wavelets are equal. (D) primary wavefront are larger than those of secondary wavelets.
›Reveal solutionSolution
Huygens' principle: in a homogeneous medium the secondary wavelets travel at the same speed as the primary wavefront, because the medium offers the same speed everywhere.
1. The concept — Huygens' principle.
Huygens' geometrical construction says:
- Every point on a primary wavefront behaves as a fresh source of disturbance, emitting secondary wavelets.
- These wavelets travel in the forward direction with the speed of the wave in that medium.
- After a time t, the new position of the wavefront is the forward envelope (common tangent) of all the secondary wavelets.
2. Why the two speeds must be identical here.
The new wavefront is constructed as the envelope of wavelets of radius vt. If the wavelets moved at some speed different from v, the envelope they build would advance at that different speed — the wavefront's speed simply is the wavelets' speed. In a homogeneous medium the speed v=c/n is the same at every point and in every direction, so:
vwavelet=vwavefront=nc
3. Why the other options fail. …
- KCET 2022Set B-31 markMCQQ.“Heat cannot be itself flow from a body at lower temperature to a body at higher temperature”. This statement corresponds to (A) Conservation of mass (B) First law of thermodynamics (C) Second law of Thermodynamics (D) Conservation of momentum
›Reveal solutionSolution
The quoted sentence is verbatim the Clausius statement of the Second Law of Thermodynamics.
Step 1 — Recognise the statement.
The sentence "heat cannot of itself flow from a body at lower temperature to a body at higher temperature" is the classic Clausius statement of the Second Law of Thermodynamics. The two crucial words are "of itself" — meaning spontaneously, with no external agency.
Step 2 — Why the First Law cannot be the answer.
The First Law is just energy conservation:
ΔQ=ΔU+ΔW
It is completely indifferent to direction. If 100 J flowed spontaneously from a cold body to a hot one, energy would still be perfectly conserved — the First Law would be entirely satisfied. Yet such a process is never observed. So the First Law is not sufficient to explain the one-way nature of heat flow; something more is needed, and that something is the Second Law.
Step 3 — What the Second Law adds: direction.
The Second Law supplies the arrow of time for thermal processes, quantified by entropy: for any spontaneous process in an isolated system,
ΔStotal≥0
If heat Q passed spontaneously from a cold reservoir at TC to a hot one at TH (with TH>TC):
ΔStotal=cold body loses−TCQ+hot body gainsTHQ=Q(TH1−TC1)<0 …
- KCET 2022Set B-31 markMCQQ.If wavelength of photon is 2.2×10−11m and h=6.6×10−34 Js , then momentum of photon (A) 1.452×10−44 kgms−1 (B) 6.89×1043 kgms−1 (C) 3×10−23 kgms−1 (D) 3.33×10−22 kgms−1
›Reveal solutionSolution
Use p=h/λ — the de Broglie / photon-momentum relation — and divide.
1. Why p=h/λ
A photon has zero rest mass, so its momentum cannot be found from p=mv. From special relativity, a massless particle satisfies E=pc; and from Planck's hypothesis its energy is E=hν. Combining, and using c=νλ:
p=cE=chν=νλhν
p=λh
(This is also exactly de Broglie's relation, read backwards — it is the same equation that assigns a wavelength to matter.)
Notice that c has cancelled: we do not need the speed of light, which is why the question only supplies h and λ.
2. Substitute
h=6.6×10−34 J s,λ=2.2×10−11 m
p=2.2×10−116.6×10−34
3. Arithmetic
Mantissas: 2.26.6=3
Exponents: 10−34−(−11)=10−23 …
- KCET 2021Set B-21 markMCQQ.A pendulum oscillates simple harmonically if and only if (I) the size of the bob of pendulum is negligible in comparison with the length of the pendulum (II) the angular amplitude is less than 10∘ (A) Both (I) and (II) are correct (B) Both (I) and (II) are incorrect (C) Only (I) is correct (D) Only (II) is correct
›Reveal solutionSolution
For a pendulum to execute simple harmonic motion, the restoring torque must be directly proportional to the angular displacement. This requires both a small bob (so it behaves as a point mass) and a small angular amplitude (so sinθ≈θ). The correct option is (A).
The key idea is that simple harmonic motion (SHM) arises only when the restoring force (or torque) is proportional to the displacement from equilibrium. For a pendulum, the restoring torque is mgLsinθ, where θ is the angular displacement. This is proportional to sinθ, not θ itself. The approximation sinθ≈θ (in radians) holds only for small angles — typically less than about 10∘. That’s why condition (II) is necessary.
But why does the bob size matter? The formula for the period T=2πL/g assumes the pendulum is a simple pendulum: a point mass suspended by a massless, inextensible string. If the bob is large, its size is not negligible compared to the length L, and the pendulum behaves as a physical pendulum — the centre of mass shifts, and the moment of inertia changes. The motion is still oscillatory, but the simple harmonic approximation fails unless the bob is small enough to treat as a point mass. So condition (I) is also necessary.
Let’s go through the reasoning step by step.
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The condition for SHM
For any oscillating system, SHM requires a restoring force (or torque) that is directly proportional to the displacement, and opposite in direction. For a pendulum, the restoring torque about the pivot is τ=−mgLsinθ. For small θ, sinθ≈θ (in radians), so τ≈−mgLθ. This is of the form τ=−kθ, which gives SHM. The approximation is accurate to within about 1% for θ<10∘ (about 0.175 rad). So condition (II) is essential.
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Why the bob size matters …
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- KCET 2020Set A-11 markMCQQ.With regard to photoelectric effect, identify the CORRECT statement among the following : (A) Number of e− ejected increases with the increase in the intensity of incident light. (B) Energy of e− ejected increases with the increase in the intensity of incident light. (C) Number of e− ejected increases with the increase in the frequency of incident light. (D) Number of e− ejected increases with the increase in work function.
›Reveal solutionSolution
In the photoelectric effect, the number of photoelectrons ejected per second is directly proportional to the intensity of incident light (for a fixed frequency above threshold), while the kinetic energy of each electron depends only on frequency and work function — not on intensity.
The photoelectric effect is a beautiful demonstration of the particle nature of light. When light of sufficient frequency (above the threshold frequency) strikes a metal surface, it ejects electrons. The key insight is that light behaves as a stream of photons, each carrying energy hν. One photon interacts with one electron, transferring its entire energy. If that energy exceeds the work function ϕ (the minimum energy needed to free the electron), the electron is ejected with kinetic energy Kmax=hν−ϕ.
This one-photon–one-electron rule is the foundation. It tells us that the number of ejected electrons depends on how many photons strike the surface per second — that is, the intensity. The energy of each ejected electron depends on the photon energy hν, not on how many photons arrive.
Let’s examine each option carefully.
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Option (A): Number of e− ejected increases with the increase in the intensity of incident light.
Intensity is energy per unit area per second. For monochromatic light, intensity I=nhν, where n is the number of photons per second per unit area. If you increase I while keeping frequency ν fixed, n increases. More photons mean more electrons ejected (provided ν is above threshold). This is correct.
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Option (B): Energy of e− ejected increases with the increase in the intensity of incident light.
The maximum kinetic energy of an ejected electron is Kmax=hν−ϕ. Intensity does not appear here. Changing intensity changes the number of photons, not the energy per photon. So the energy of each electron remains the same. This is false.
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Option (C): Number of e− ejected increases with the increase in the frequency of incident light. …
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