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Biomacromolecules

BiologyBiomolecules (Biology)For NEET aspirants

Biomacromolecules are the large molecules of living tissue that collect in the acid-insoluble fraction: proteins, nucleic acids and polysaccharides, with lipids separating alongside them. This page explains why lipids fall in this fraction, the average composition of a cell, proteins and their functions, polysaccharides such as cellulose, starch, glycogen, inulin and chitin, nucleic acids, and the four levels of protein structure, as in the NCERT Class 11 chapter Biomolecules. NEET asks biomacromolecules mostly as statement sets and match lists.

On this page1Acid-insoluble fraction2Proteins3Polysaccharides4Nucleic acids5Structure of proteins6Exam essentials7Practice
Key Points at a Glance
  1. ★ Must learn Acid-soluble pool: molecular weights from 18 to about 800 Da. Acid-insoluble fraction: proteins, nucleic acids, polysaccharides and lipids.
  2. Micromolecules are below 1000 Da; macromolecules (except lipids) are 10,000 Da and above.
  3. ★ Must learn Lipids come down with the insoluble fraction as membrane vesicles; they are not strictly macromolecules.
  4. Water is the most abundant chemical in living organisms: 70-90% of cell mass.
  5. Proteins are heteropolymers of 20 types of amino acids joined by peptide bonds.
  6. ★ Must learn Collagen: most abundant protein in the animal world. RuBisCO: most abundant protein in the whole biosphere.
  7. Cellulose is a homopolymer of glucose; starch (plants) and glycogen (animals) are its variants; inulin is a polymer of fructose.
  8. Starch forms helices that hold (blue); cellulose cannot. Chitin forms the arthropod exoskeleton.
  9. ★ Must learn Nucleotide = nitrogenous base + pentose sugar + phosphate; DNA has deoxyribose, RNA has ribose.
  10. ★ Must learn Protein structure: primary (sequence), secondary (helix), tertiary (folded ball), quaternary (subunits). Adult human haemoglobin = 2 + 2 .

1. The Acid-insoluble Fraction

1.1 Micromolecules and macromolecules

  • ★ Exam imp All compounds of the acid-soluble pool have molecular weights from 18 to around 800 daltons (Da).
  • The acid-insoluble fraction has only four types of organic compounds: proteins, nucleic acids, polysaccharides and lipids.
  • Except lipids, these classes have molecular weights of ten thousand daltons and above.
  • For this reason, biomolecules (chemical compounds of living organisms) are of two types.
  • ★ Exam imp Except lipids, the molecules of the insoluble fraction are polymeric substances.
Micromolecules (biomolecules)
  • Molecular weight less than one thousand daltons.
  • Found in the acid-soluble pool.
Macromolecules (biomacromolecules)
  • Found in the acid-insoluble fraction.
  • Proteins, nucleic acids and polysaccharides: 10,000 Da and above, polymers.

1.2 Why lipids appear in the insoluble fraction

Lipids have molecular weights that do not exceed 800 Da, yet they come down with the macromolecules:

  1. Lipids are small molecules. They occur as such and are also arranged into the cell membrane and other membranes.
  2. Grinding a tissue disrupts the cell structure, and the membranes break into pieces.
  3. The pieces form vesicles, which are not water soluble.
  4. These vesicles separate along with the acid-insoluble pool, so lipids appear in the macromolecular fraction.

★ Very important Lipids are not strictly macromolecules. Only proteins, nucleic acids and polysaccharides are true macromolecules; lipids reach the insoluble fraction only because of their membranes.

1.3 Average composition of a cell

  • The acid-soluble pool represents roughly the cytoplasmic composition.
  • The macromolecules from the cytoplasm and organelles form the acid-insoluble fraction.
  • Together, the two fractions represent the entire chemical composition of living tissues or organisms.
  • ★ Exam imp Arranged class-wise by abundance, water is the most abundant chemical in living organisms.
Component% of the total cellular mass
Water70-90
Proteins10-15
Carbohydrates3
Lipids2
Nucleic acids5-7
Ions1
Memory Trick

Decreasing order: "Wise People Never Count Little Ions" = Water (70-90), Proteins (10-15), Nucleic acids (5-7), Carbohydrates (3), Lipids (2), Ions (1).

Key idea
Three true macromolecules (proteins, nucleic acids, polysaccharides) and the membrane lipids form the insoluble fraction, while water dominates the cell by mass.

2. Proteins

  • ★ Exam imp Proteins are polypeptides: linear chains of amino acids linked by peptide bonds (Figure 2).
  • Each protein is a polymer of amino acids.
  • There are 20 types of amino acids, for example alanine, cysteine, proline, tryptophan and lysine.
  • ★ Exam imp So a protein is a heteropolymer, not a homopolymer.
  • Homopolymer: a polymer in which only one type of monomer repeats 'n' number of times.
  • Certain amino acids are essential for our health and must be supplied through the diet. Dietary proteins are the source of these essential amino acids.
Essential amino acids

Cannot be made by the body; obtained through our diet or food.

Non-essential amino acids

Our body can make them.

  • Proteins carry out many functions: some transport nutrients across the cell membrane, some fight infectious organisms, some are hormones and some are enzymes.
ProteinFunction
CollagenIntercellular ground substance
TrypsinEnzyme
InsulinHormone
AntibodyFights infectious agents
ReceptorSensory reception (smell, taste, hormone, etc.)
GLUT-4Enables glucose transport into cells

★ Very important Collagen is the most abundant protein in the animal world; RuBisCO (Ribulose bisphosphate Carboxylase-Oxygenase) is the most abundant protein in the whole biosphere.

Memory Trick

Collagen Crowns the animals; RuBisCO Rules the biosphere. GLUT-4 lets GLUcose in. Trypsin is a Tool (enzyme); Insulin is an Instruction (hormone).

NEET Focus

Watch the word "most abundant". Animal world: collagen. Whole biosphere: RuBisCO. Most abundant chemical in a cell: water. Also: a protein is a heteropolymer, while cellulose is a homopolymer.

Key idea
Proteins are heteropolymers of 20 amino acids that work as enzymes, hormones, antibodies, receptors, transporters and structural material.

3. Polysaccharides

  • The acid-insoluble pellet also has polysaccharides (carbohydrates), another class of macromolecules.
  • ★ Exam imp Polysaccharides are long chains of sugars: threads (literally like a cotton thread) with different monosaccharides as building blocks.
  • Cellulose is a polymeric polysaccharide made of only one type of monosaccharide, glucose. So cellulose is a homopolymer.
  • Starch is a variant of this, present as a store house of energy in plant tissues.
  • Animals have another variant called glycogen.
  • ★ Exam imp Inulin is a polymer of fructose.
  • In a polysaccharide chain (say glycogen), the right end is the reducing end and the left end the non-reducing end.
  • Glycogen has branches, as shown in the cartoon (Figure 1).
Diagrammatic representation of a portion of glycogen A cartoon of glycogen as a long chain of glucose units with several side branches. Two boxed areas are enlarged below. The left view shows a branch point: glucose rings joined by oxygen bridges in a row, with a side chain attached through an oxygen to the CH2 group of one ring. The right view shows an unbranched stretch: rings with CH2OH and OH groups joined through oxygen bridges, the last ring on the right carrying a free OH. O O O O O O O O CH2 O O O O CH2OH OH OH O CH2OH OH OH O CH2OH OH OH OH O O O
Figure 1: A portion of glycogen: a branched chain of glucose units. Left: a branch point, where a side chain joins through O to the of a ring. Right: an unbranched stretch of rings joined by O bridges.
  • ★ Exam imp Starch forms helical secondary structures and can hold molecules in the helical portion. The starch- is blue.
  • Cellulose does not contain complex helices, so it cannot hold .
  • Plant cell walls are made of cellulose. Paper made from plant pulp and cotton fibre are cellulosic.
  • More complex polysaccharides have amino-sugars and chemically modified sugars as building blocks, for example glucosamine and N-acetyl galactosamine.
  • ★ Exam imp The exoskeleton of arthropods has a complex polysaccharide called chitin. These complex polysaccharides are mostly homopolymers.
  • Polysaccharides form the cell walls of plants and fungi and the exoskeleton of arthropods. Starch and glycogen are storage forms of energy.
PolysaccharideBuilding blockWhere and why it matters
CelluloseGlucose only (homopolymer)Plant cell walls; paper and cotton fibre; cannot hold
StarchGlucose (variant of cellulose)Energy store in plant tissues; helical; starch- is blue
GlycogenGlucose (variant)Found in animals; branched chain
InulinFructoseA polymer of fructose
ChitinAmino-sugars, modified sugarsExoskeleton of arthropods; complex polysaccharide
Memory Trick

Starch Spirals, so it Stores iodine (blue); cellulose is Straight, so it cannot. Inulin is the odd one out: fructose, not glucose.

Quick Recall: tap to check
Which polysaccharide is a polymer of fructose?
Inulin.
Which end of a glycogen chain is the reducing end?
The right end; the left end is the non-reducing end.
Name two building blocks of complex polysaccharides.
Glucosamine and N-acetyl galactosamine (amino-sugars and modified sugars).
Which complex polysaccharide forms the exoskeleton of arthropods?
Chitin.
Tips and Tricks

To tell plant and animal storage forms apart: Starch Stays in plants; Glycogen Goes with animals. For "which is NOT a glucose polymer", look for inulin; for "which cannot hold iodine", look for cellulose.

Key idea
Glucose builds cellulose (walls), starch (plant store) and branched glycogen (animal store); fructose builds inulin; modified sugars build chitin.

4. Nucleic Acids

  • ★ Exam imp Nucleic acids are polynucleotides, found in the acid-insoluble fraction of every living tissue.
  • Together with polysaccharides and polypeptides, they form the true macromolecular fraction of any living tissue or cell.
  • The building block of a nucleic acid is a nucleotide.
  • A nucleotide has three chemically distinct components: a heterocyclic compound, a monosaccharide, and phosphoric acid or phosphate.
  • The heterocyclic compounds are the nitrogenous bases: adenine, guanine, uracil, cytosine and thymine.
  • ★ Exam imp Adenine and guanine are substituted purines; uracil, cytosine and thymine are substituted pyrimidines.
  • The skeletal heterocyclic rings are called purine and pyrimidine respectively.
  • The sugar is either ribose (a monosaccharide pentose) or 2′-deoxyribose.
  • Nucleic acids serve as genetic material; they carry hereditary information from the parental generation to the progeny.
DNA: deoxyribonucleic acid

Contains the sugar deoxyribose (2′-deoxyribose).

RNA: ribonucleic acid

Contains the sugar ribose.

★ Very important Nucleotide = nitrogenous base + pentose sugar + phosphate. Purines: adenine and guanine. Pyrimidines: uracil, cytosine and thymine.

Memory Trick

"Pure As Gold": Purines are Adenine and Guanine. "CUT the Py": Cytosine, Uracil, Thymine are Pyrimidines.

Key idea
A nucleic acid is a chain of nucleotides; each nucleotide carries a purine or pyrimidine base, a ribose or deoxyribose sugar and a phosphate.

5. Structure of Proteins

  • Proteins are heteropolymers containing strings of amino acids.
  • 'Structure of a molecule' means different things in different contexts:
FieldWhat 'structure' meansExample
Inorganic chemistryMolecular formula,
Organic chemistryA two-dimensional view of the moleculeBenzene, naphthalene
PhysicsThree-dimensional views of molecular structure-
BiologyProtein structure at four levelsPrimary to quaternary

Biologists describe protein structure at four levels:

  1. Primary structure: the sequence of amino acids, that is, the positional information (which amino acid is first, which second, and so on). The protein is imagined as a line: the left end is the first amino acid (N-terminal) and the right end the last amino acid (C-terminal).
  2. Secondary structure: the thread is not an extended rigid rod. Some portions fold into a helix, like a revolving staircase; only right-handed helices occur in proteins. Other regions fold into other forms.
  3. Tertiary structure: the long chain is folded upon itself like a hollow woollen ball. This gives a three-dimensional view of the protein.
  4. Quaternary structure: some proteins are an assembly of more than one polypeptide or subunit. The arrangement of the folded subunits with respect to each other (a linear string of spheres, or spheres stacked as a cube or plate) is the protein's architecture.
Levels of protein structure Four levels of protein structure in a grid: (a) primary, a chain of amino acid units forming a polypeptide; (b) secondary, the chain coiled into a right-handed alpha helix and folded into a zigzag beta-pleated sheet; (c) tertiary, the chain folded on itself into a compact ball, with hydrogen bonds and a disulphide bond marked between neighbouring strands; (d) quaternary, four folded subunits packed together into one protein (a) (b) (c) (d) Primary Secondary Tertiary Quaternary Polypeptide Alpha helix Beta-pleatedsheet Disulphidebond Hydrogenbond Subunits
Figure 2: Levels of protein structure: (a) primary, a polypeptide chain; (b) secondary, the alpha helix and the beta-pleated sheet; (c) tertiary, a chain folded on itself and held by hydrogen bonds and disulphide bonds; (d) quaternary, folded subunits packed together.
  • ★ Exam imp Adult human haemoglobin has 4 subunits: two identical subunits and two identical subunits.

★ Very important Tertiary structure is absolutely necessary for the many biological activities of proteins. It gives the protein its three-dimensional shape.

Memory Trick

Four levels, four S words: Sequence (primary), Spiral (secondary), Sphere of wool (tertiary), Subunits (quaternary).

NEET Focus

Common statement traps: only right-handed helices occur in proteins; only some portions of the chain are helical; the first amino acid is N-terminal; adult human haemoglobin has 2 + 2 subunits (four in all), so it shows quaternary structure.

Quick Recall: tap to check
In the protein structure figure, which level shows the alpha helix and the beta-pleated sheet?
Secondary structure.
Which two bonds are marked in the tertiary structure?
Hydrogen bond and disulphide bond.
Which level of structure does a single polypeptide chain of amino acids show?
Primary structure.
In the glycogen figure, what links a side chain to the main chain at a branch point?
An oxygen bridge to the group of a glucose ring.
Key idea
Sequence fixes the primary structure; local helices make the secondary, the folded ball the tertiary, and the packing of subunits the quaternary structure.

6. Exam Essentials

Pairs to Match

List IList II
Acid-soluble poolMolecular weights of 18 to about 800 Da
Acid-insoluble fractionProteins, nucleic acids, polysaccharides, lipids
CollagenIntercellular ground substance; most abundant protein in animals
TrypsinEnzyme
InsulinHormone
AntibodyFights infectious agents
ReceptorSensory reception (smell, taste, hormone)
GLUT-4Glucose transport into cells
RuBisCOMost abundant protein in the biosphere
CelluloseHomopolymer of glucose; plant cell wall
InulinPolymer of fructose
ChitinExoskeleton of arthropods
Starch-Blue colour
Adenine and guaninePurines
Adult human haemoglobinTwo and two subunits

Exceptions

  • Lipids are in the acid-insoluble fraction but are not strictly macromolecules (molecular weight not above 800 Da).
  • All classes of the insoluble fraction except lipids are polymers of 10,000 Da and above.
  • A protein is a heteropolymer, unlike cellulose, which is a homopolymer.
  • Inulin is a polymer of fructose, not glucose.
  • Cellulose cannot hold iodine, unlike starch.
  • Only right-handed helices are observed in proteins, and only some portions of the chain are helical.
  • Complex polysaccharides such as chitin are built of modified sugars, yet are mostly homopolymers.

Numbers to Remember

  • Acid-soluble pool: 18 to about 800 Da; lipids: not above 800 Da.
  • Micromolecules: less than 1000 Da; macromolecules (except lipids): 10,000 Da and above.
  • Cell mass: water 70-90%, proteins 10-15%, nucleic acids 5-7%, carbohydrates 3%, lipids 2%, ions 1%.
  • 20 types of amino acids; 4 classes in the insoluble fraction; 3 true macromolecules.
  • Protein structure: 4 levels. Adult human haemoglobin: 4 subunits (2 + 2 ).
  • Nucleotide: 3 components. Bases: 2 purines and 3 pyrimidines.

Examples to Remember

GroupExamples
Proteins with functionsCollagen, trypsin, insulin, antibody, receptor, GLUT-4, RuBisCO, haemoglobin
Amino acids namedAlanine, cysteine, proline, tryptophan, lysine
Glucose polymersCellulose, starch, glycogen
Fructose polymerInulin
Modified sugarsGlucosamine, N-acetyl galactosamine (building blocks of complex polysaccharides)
Cellulosic productsPaper from plant pulp, cotton fibre
Purines / pyrimidinesAdenine, guanine / uracil, cytosine, thymine
Structure views, (formulae); benzene, naphthalene (2-D views)

7. Quick Revision

  • Acid-soluble pool: 18 to about 800 Da; acid-insoluble fraction: proteins, nucleic acids, polysaccharides, lipids.
  • Micromolecules are below 1000 Da; macromolecules (except lipids) are 10,000 Da and above and are polymers.
  • Lipids come down as membrane vesicles, so they are not strictly macromolecules.
  • The soluble pool roughly equals the cytoplasm; both fractions together give the whole composition.
  • Water is the most abundant chemical: 70-90% of cell mass.
  • Proteins are heteropolymers of 20 amino acids linked by peptide bonds.
  • Essential amino acids come from the diet; non-essential ones are made by the body.
  • Collagen is most abundant in animals; RuBisCO in the whole biosphere.
  • Cellulose (glucose homopolymer), starch (plants), glycogen (animals, branched), inulin (fructose), chitin (arthropods).
  • Starch helices hold iodine and turn blue; cellulose cannot.
  • In glycogen, the right end is reducing and the left end non-reducing.
  • Nucleotide = heterocyclic base + monosaccharide + phosphate; A and G are purines; U, C and T are pyrimidines.
  • DNA has deoxyribose; RNA has ribose; nucleic acids are genetic material.
  • Primary (sequence, N- to C-terminal), secondary (right-handed helix), tertiary (woollen ball), quaternary (subunits).
  • Adult human haemoglobin: 2 + 2 subunits.

8. Solved Examples

Solved Example 1
Match List I with List II.
List I: A. Collagen; B. Trypsin; C. GLUT-4; D. Receptor
List II: I. Sensory reception; II. Intercellular ground substance; III. Enzyme; IV. Glucose transport into cells
Choose the correct answer.
(A) A-II, B-III, C-IV, D-I
(B) A-III, B-II, C-IV, D-I
(C) A-II, B-III, C-I, D-IV
(D) A-IV, B-III, C-II, D-I
Solution:

Answer: (A). Collagen forms intercellular ground substance (II), trypsin is an enzyme (III), GLUT-4 enables glucose transport (IV) and receptors serve sensory reception (I).

Solved Example 2
Read the statements about polysaccharides.
A. Cellulose is a homopolymer of glucose.
B. Inulin is a polymer of glucose.
C. Starch can hold in its helical portion and turns blue.
D. Chitin is a complex polysaccharide of the arthropod exoskeleton.
E. Cellulose forms complex helices that hold iodine.
Choose the correct answer.
(A) A, C and D only
(B) A, B and C only
(C) B, D and E only
(D) A, C, D and E only
Solution:

Answer: (A). B is false: inulin is a polymer of fructose. E is false: cellulose has no complex helices and cannot hold .

Solved Example 3
Arrange the levels of protein structure from the simplest to the most complex.
A. Folding of the chain upon itself into a hollow woollen ball
B. Sequence of amino acids
C. Arrangement of several folded subunits
D. Helix in some portions of the chain
Choose the correct order.
(A) B, D, A, C
(B) B, A, D, C
(C) D, B, A, C
(D) B, D, C, A
Solution:

Answer: (A). Primary (sequence), secondary (helix), tertiary (woollen ball), quaternary (subunits).

Solved Example 4
The most abundant protein in the whole biosphere is:
(A) Collagen
(B) Haemoglobin
(C) RuBisCO
(D) Insulin
Solution:

Answer: (C). RuBisCO. Collagen is the most abundant protein only in the animal world.

Solved Example 5
Which of the following is NOT a true macromolecule, even though it is found in the acid-insoluble fraction?
(A) Protein
(B) Nucleic acid
(C) Polysaccharide
(D) Lipid
Solution:

Answer: (D). Lipids do not exceed 800 Da. They come down only as water-insoluble membrane vesicles.

Solved Example 6
Statement I: In proteins, only right-handed helices are observed.
Statement II: Adult human haemoglobin consists of three subunits and one subunit.
Choose the correct answer.
(A) Both Statement I and Statement II are correct
(B) Both Statement I and Statement II are incorrect
(C) Statement I is correct but Statement II is incorrect
(D) Statement I is incorrect but Statement II is correct
Solution:

Answer: (C). Statement II is wrong: adult human haemoglobin has two and two subunits.

9. Practice Questions

Practice Questions
  1. Match List I with List II.
    List I: A. Cellulose; B. Glycogen; C. Inulin; D. Chitin
    List II: I. Polymer of fructose; II. Exoskeleton of arthropods; III. Plant cell walls; IV. Branched polysaccharide of animals
    Choose the correct answer.
    (1) A-III, B-IV, C-I, D-II
    (2) A-IV, B-III, C-I, D-II
    (3) A-III, B-I, C-IV, D-II
    (4) A-III, B-IV, C-II, D-IAnswer: (1). Cellulose: plant cell walls; glycogen: animals, branched; inulin: fructose; chitin: arthropod exoskeleton.
  2. Read the statements about the acid-insoluble fraction.
    A. It contains proteins, nucleic acids, polysaccharides and lipids.
    B. All its compounds have molecular weights below 800 Da.
    C. Except lipids, its compounds are polymers.
    D. It represents roughly the cytoplasmic composition.
    E. Lipids reach it as water-insoluble membrane vesicles.
    Choose the correct answer.
    (1) A, C and E only
    (2) A, B and D only
    (3) B, C and E only
    (4) A, C, D and E onlyAnswer: (1). B is false: except lipids they are 10,000 Da and above. D is false: the acid-soluble pool represents the cytoplasm.
  3. Arrange these cell components in decreasing order of their share of cell mass.
    A. Proteins; B. Lipids; C. Water; D. Nucleic acids
    (1) C, A, D, B
    (2) C, D, A, B
    (3) A, C, D, B
    (4) C, A, B, DAnswer: (1). Water 70-90, proteins 10-15, nucleic acids 5-7, lipids 2 per cent.
  4. Which of the following is NOT a pyrimidine?
    (1) Cytosine
    (2) Uracil
    (3) Guanine
    (4) ThymineAnswer: (3). Guanine is a purine, like adenine.
  5. Starch gives a blue colour with iodine because:
    (1) it is a polymer of fructose
    (2) its helical portion holds molecules
    (3) it is a heteropolymer
    (4) it is branched like glycogenAnswer: (2). Starch forms helical secondary structures that hold .
  6. Statement I: The first amino acid of a protein is called the N-terminal amino acid.
    Statement II: Tertiary structure gives a three-dimensional view of a protein.
    Choose the correct answer.
    (1) Both Statement I and Statement II are correct
    (2) Both Statement I and Statement II are incorrect
    (3) Statement I is correct but Statement II is incorrect
    (4) Statement I is incorrect but Statement II is correctAnswer: (1). Both are correct.
  7. Dietary proteins are important mainly because they supply:
    (1) non-essential amino acids
    (2) essential amino acids
    (3) nucleotides
    (4) fatty acidsAnswer: (2). Essential amino acids cannot be made by the body and must come through the diet.
Review Questions
  1. What are macromolecules? Give examples.Answer: Macromolecules are the large compounds of the acid-insoluble fraction, with molecular weights of 10,000 Da and above. They are polymers: proteins, nucleic acids and polysaccharides (for example collagen, DNA and cellulose). Lipids also separate in this fraction but are not strictly macromolecules.
  2. What is meant by the tertiary structure of proteins?Answer: The long protein chain folds upon itself like a hollow woollen ball. This three-dimensional shape is the tertiary structure, and it is absolutely necessary for many biological activities of proteins.
  3. Make a list of proteins used as therapeutic agents. Find other uses of proteins, such as in cosmetics.Answer: Therapeutic: insulin, antibodies, interferons, blood-clotting factors and the clot-dissolving enzyme streptokinase. Other uses: collagen and keratin in cosmetics, enzymes in detergents, and gelatin in foods and capsules.
  4. What are gums made of? Is Fevicol different?Answer: Gums are polymeric secondary metabolites of plants, made mostly of complex polysaccharides. Fevicol is different: it is a synthetic adhesive based on polyvinyl acetate, not a natural biomolecule.
  5. Compare how much cellulose plants make with how much paper humans make. What does this mean for vegetation?Answer: Estimates vary, but plants make roughly tonnes of cellulose a year, while world paper production is only a few hundred million tonnes. Paper uses a small share of the cellulose made, but most of it comes from felled trees, so the real loss is in forest cover.

Common Mistakes to Avoid

Watch out
  • Calling lipids true macromolecules. They are small (not above 800 Da) and only come down as membrane vesicles.
  • Writing that a protein is a homopolymer. It is a heteropolymer of 20 types of amino acids.
  • Taking inulin as a glucose polymer. Inulin is a polymer of fructose.
  • Saying cellulose turns blue with iodine. Only starch, with its helices, holds .
  • Calling collagen the most abundant protein of the biosphere. That is RuBisCO; collagen leads only in animals.
  • Writing that proteins have left-handed helices. Only right-handed helices are observed.
  • Calling the last amino acid N-terminal. The first is N-terminal; the last is C-terminal.
  • Listing uracil or thymine as a purine. Only adenine and guanine are purines.

Frequently Asked Questions

What are biomacromolecules?

Biomacromolecules are the large molecules of living tissue found in the acid-insoluble fraction. Proteins, nucleic acids and polysaccharides are true macromolecules, with molecular weights of ten thousand daltons and above. They are polymers made of different building blocks: amino acids, nucleotides and monosaccharides.

Why are lipids found in the acid-insoluble fraction?

Lipids are small, with molecular weights not above 800 Da, but they form the cell membrane and other membranes. Grinding breaks these membranes into pieces that form water-insoluble vesicles. The vesicles separate with the acid-insoluble pool, so lipids appear there though they are not strictly macromolecules.

Which is the most abundant protein in the biosphere?

Ribulose bisphosphate carboxylase-oxygenase, or RuBisCO, is the most abundant protein in the whole biosphere. Collagen is the most abundant protein in the animal world. The most abundant chemical in living organisms is water, which forms 70 to 90 per cent of cell mass.

Why is a protein called a heteropolymer?

A protein is a polymer of amino acids, and 20 different types of amino acids can occur in it, such as alanine, cysteine, proline, tryptophan and lysine. A homopolymer has only one type of monomer repeating many times. Cellulose, made only of glucose, is an example of a homopolymer.

Why does starch turn blue with iodine but cellulose does not?

Starch forms helical secondary structures, and iodine molecules can sit in the helical portion. The starch-iodine complex is blue. Cellulose does not contain complex helices, so it cannot hold iodine and gives no blue colour. This is why the iodine test can tell starch from cellulose.

What are the components of a nucleotide?

A nucleotide has three chemically distinct parts: a heterocyclic nitrogenous base, a pentose sugar and a phosphate. The base is a purine (adenine or guanine) or a pyrimidine (cytosine, uracil or thymine). The sugar is ribose in RNA and deoxyribose in DNA.

What is the tertiary structure of a protein?

In the tertiary structure, the long protein chain is folded upon itself like a hollow woollen ball. This gives the protein its three-dimensional shape. Tertiary structure is absolutely necessary for the many biological activities of proteins, including the active sites of enzymes.

What is the quaternary structure of haemoglobin?

Quaternary structure is the arrangement of two or more folded polypeptide subunits with respect to each other. Adult human haemoglobin has four subunits: two identical alpha subunits and two identical beta subunits, packed together as one functional protein. Proteins made of a single folded chain show structure only up to the tertiary level.

Previous year questions on Biomacromolecules

11 questions from past papers, each with a step-by-step solution.

Show all 11 questions

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