NCERT Class 11 Biology Biomolecules Important Notes

Analysis Of Chemical Composition: For this, a living tissue is taken. The tissue is ground in trichloroacetic acid (Cl₃CCOOH); by using pestle and mortar. The slurry is then filtered through a cloth. The filtrate contains acid-soluble pool and the retentate contains acid-insoluble fraction. Organic compounds are found in the acid-soluble pool, while inorganic substances are found in acid-insoluble fraction.

Biomolecules: All the carbon compounds which are obtained from living tissues are called biomolecules.

AMINO ACIDS:

Amino acids are organic compounds which contain an amino group and an acidic group as substituents on the same carbon, i.e. α-carbon. Due to this, they are called α-amino acids. The amino acids are substituted methanes. There are four substituent groups which occupy the four valency positions. These groups are; hydrogen, carboxyl group, amino group and a variable group; called R group. The nature of the R-group governs a particular type of amino acids.

However, there are only 21 types of amino acids which occur in proteins. The R-group in these proteinaceous amino acids could be of various types. The amino, carboxyl and the R functional groups decide the chemical and physical properties of an amino acid.

Amino acid with a hydrogen is called glycine, one with a methyl group is called alanine, one with hydroxyl methyl group is called serine, etc. Based on the number of amino and carboxyl group, the amino acids can be acidic, basic or neutral. A particular feature of amino acid is the ionizable nature of –NH₂ and –COOH groups. Hence, structure of amino acids changes in solutions of different pH.

LIPIDS:

Lipids are usually insoluble in water. Lipids can be simple fatty acids and some lipids have phosphorous and phosphorylated organic compounds in them. Lipids; containing phosphorus; are called phospholipids. A fatty acid has a carboxyl group attached to an R group. The R group can be a methyl or ethyl or higher number of CH₂ group (1 carbon to 19 carbons).

Fatty acids could be saturated or unsaturated. Many lipids have both glycerol and fatty acids. In this case, the fatty acids are found esterified with glycerol. They can be monoglycerides, diglycerides and triglycerides. On the basis of melting points, they can be termed as fats and oils. Oils have lower melting points while fats have higher melting points.

There are a number of carbon compounds; with heterocylic rings; found in living organisms. Some of them are nitrogenous bases, e.g. adenine, guanine, cytosine, uracil and thymin. When a nitrogenous base is attached to a sugar, it is called a nucleoside, e.g. adenosine, guanosine, thymidine, uridine and cytidine. If a phosphate group is also found esterified to the sugar then they are called nucleotides, e.g. adenylic acid, thymidylic acid, guanylic acid, uridylic acid and cytidylic acid.

Primary Metabolites: Metabolites which have identifiable functions are called primary metabolites. They play known key roles in normal physiological processes. All the primary metbaolites are found in animal cells.

Secondary Metabolites: There are certain metabolites about which we do not have enough information to suggest their role in physiological processes. Such metabolites are called secondary metabolites. Secondary metabolites are not found in animal cells.

Mircomolecules: Biomolecules with molecular eights less than one thousand Dalton are called micromolecules or simple as biomolecules.

Biomacromolecules: Biomolecules with molecular weights more than one thousand Dalton are called biomacromolecules. These are found in the acid-insoluble fraction.

Proteins

Protein is a polymer of amino acids. Based on similar or different monomers repeating in a protein, it is classified as homopolymer and heteropolymer. When same monomer is repeated in the protein, it is called homopolymer. When different monomers are present in the protein, it is called heteropolymer.

Essential Amino Acids: Some amino acids are essential for our health. But our body does not make them and they need to be supplemented through diet. Such amino acids are called essential amino acids. Collagen is the most abundant protein in the animal world. Ribulose biphosphate Carboxylase-Oxygenae (RUBISCO) is the most abundant protein in the whole biosphere.

POLYSACCHARIDES

The long chains of sugars are called polysachharides. If a polysaccharide is made up of similar monosaccharides, it is called homopolymer, e.g. cellulose. If a polysaccharide is made up of different monosachharides, it is called heteropolymer.

The right end of a polysaccharide chain is called the reducing end and the left end is called the non-reducing end.

Starch forms helical secondary structures. Starch can hold I2 (iodine) molecules in helical portion. Cellulose does not contain complex helices and hence cannot hold I2 .

In a polysaccharide chain, the right end is called the reducing end and the left end is called the non-reducing end. Starch forms helical secondary structures. In fact, starch can hold I2 molecules in the helical portion.

NUCLEIC ACIDS

A nucleic acid is composed of nucleotide. There are three chemically distinct components in a nucleotide. One of them is a heterocyclic compound, the second is a monosaccharide and the third is phosphoric acid or phosphate.

The heterocyclic compounds; present in nucleic acids are the nitrogenous bases, viz. adenine, guanine, uracil, cytosil and thymine. Adenine and Guanine are substituted purines, while uracil, cytosil and thymine are substituted pyrimidines.

Based on the presence of purine or pyrimidine, the heterocyclic ring is called purine and pyrimidine. Polynucleotides contain either ribose sugar or 2’ deoxyribose sugar. If ribose sugar is present then the nucleic acid is called ribonucleic acid (RNA). If deoxyribose sugar is present then the nucleic acid is called deoxyribose nucleic acid (DNA).

STRUCTURE OF PROTEINS

Primary Structure: The sequence of amino acids is called the primary structure of a protein. The left end is represented by the first amino acid, while the right end is represented by the last amino acid. The first amino acid is also called N-terminal amino acid. The last amino acid is called C-terminal amino acid.

Secondary Structure: The protein is not a linear chain of amino acids rather the chain would bend at some places and even form helices. Regularly repeating local structures gives secondary structure to protein.

Tertiary Structure: The overall shape of a protein molecule; and the spatial relationship of the secondary structures to one another; is called tertiary structure of protein. In other words, the various folds which give three dimensional appearances to protein form its tertiary structure.

Quaternary Structure: The manner in which the individual folded polypeptides are arranged with respect to each other is called quaternary structure of protein.

NATURE OF BOND LINKING MONOMERS IN A POLYMER

Glycosidic Bond: Certain type of functional group which joins a sugar molecule to another group is called glycosidic bond. Another group may or may not be another carbohydrate.

Peptide Bond: A chemical bond formed between two molecules; when the carboxyl group of one molecule reacts with the amine group of another molecule; is called peptide bond (amide bond). A molecule of water is released during this reaction. This is a dehydration synthesis reaction and usually occurs between two amino acids. This is also known as a condensation reaction. The resulting CO – NH bond is called a peptide bond. The resulting molecule is called an amide. The four atom functional group – C (=O)NH – is called an amide group or a peptide group.

Phospho-diester Bond: A group of strong covalent bonds between a phosphate group and two other molecules over two ester bonds is called a phosphor-diester bond. Phosphodiester bonds make the backbone of the strands of DNA and hence are central to all life on Earth. In DNA and RNA, the phosphodiester bond is the linkage between the 3’ carbon atom of one sugar molecule and the 5’ carbon atom of another.

DYNAMIC STATE OF BODY CONSTITUENTS – CONCEPT OF METABOLISM

Metabolism: All the biomolecules are constantly being changed into some other biomolecules and also made from some other biomolecules. The turnover of biomolecules takes place continuously. All these reactions are together called metabolism.

Anabolism:When a complex biomolecule is synthesized from simple biomolecules through a biological process, the process is called anabolism. Energy is utilised during anabolism.

Catabolism: When a complex biomolecule is disintegrated to produce simple biomolecules through a biological process, the process is called catabolism. Energy is released during catabolism.

Metabolic Pathway: Metabolites are converted into each other in a series of linked reactions. Such a series of linked reactions is called metabolic pathway. Every chemical reaction in the metabolic pathways is a catalysed reaction. The metabolic pathways are either linear or circular. These pathways crisscross each other; which means there are traffic junctions. But the interlinked metabolic traffic is very smooth and no single mishap has been reported for healthy conditions.

The Living State: All living organisms exist in a steady state; characterized by concentrations of each of the biomolecules. The steady state is a non-equilibrium state. It can be said that the living process is a constant effort to prevent falling into equilibrium. Without metabolism, there cannot be a living state.

ENZYMES

An enzyme is a catalyst which is utilised in metabolic reactions. Almost all enzymes are proteins.

"Lock and Key" Model: The lock and key model was suggested by Emil Fischer in 1894. Emil Fischer postulated that both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another. This model explains the specificity of enzyme. But this model fails to explain the stabilization of the transition state which an enzyme achieves.

Induced Fit Model: This is the most accepted model and is a modification over the lock and key model. The induced fit model was proposed by Daniel Koshland in 1958. According to this model, since enzymes are rather flexible structures; the active site is continually reshaped by interactions with the substrate when the substrate interacts with the enzyme. In some cases, the substrate molecule also changes shape slightly when it enters the active site. The active site continues to change until the substrate is completely bound. The final shape and charge is determined at this point of enzyme-substrate reaction.

There are many differences between enzyme catalysts and inorganic catalysts. Inorganic catalysts work efficiently at high temperatures and high pressures, enzymes get damaged at high temperatures (above 40°C). But enzymes which are isolated from thermophilic organisms show thermal stability.

Mechanisms of Enzymatic Actions

• Enzyme lowers the activation energy by creating an environment in which the transition state is stabilized.

• Enzyme lowers the energy of the transition state by creating an environment with the opposite charge distribution to that of the transition state. But an enzyme does this without distorting the substrate.

• Enzyme provides an alternative pathway.

• Enzyme reduces the reaction entropy charge by bringing substrates together in the correct orientation to react.

• Increase in temperatures speeds up reactions. But if the enzyme is heated too much, its shape deteriorates and it regains it shape only when the temperature comes back to normal. Some enzymes work best at low temperatures, e.g. thermolabile.

The catalytic cycle of an enzyme action can be described in the following steps:

1. The substrate binds to the active site of the enzyme, fitting into the active site.

2. The binding of the substrate induces the enzyme to alter its shape, fitting more tightly around the substrate.

3. The active site of the enzyme breaks the chemical bonds of the substrate and the new enzyme- product complex is formed.

4. The enzyme releases the products of the reaction and the free enzyme is ready to bind to another molecule of the substrate.

Factors Affecting Enzyme Activity

Temperature and pH: Enzymes usually function in a narrow range of temperature and pH. Each enzyme shows its highest activity at optimum temperature and optimum pH. Beyond that range, the activity declines. Low temperature preserves the enzyme temporarily in inactive state, while high temperature destroys the enzyme.

Concentration of Substrate: The velocity of enzymatic action at first rises with an increase in substrate concentration. But the velocity of reaction does not rise once it reaches a maximum velocity (Vmax). This happens because there are fewer molecules of enzyme and no free enzyme molecule is left to bind with the additional substrate molecules.

Effect of Inhibitor: When the inhibitor closely resembles the substrate and inhibits the activity of an enzyme, it is known as competitive inhibitor. Because of its close structural similarity with the substrate, the inhibitor competes with the substrate for the binding site on the enzyme. Such competitive inhibitors are often used in the control of bacterial pathogens.

Classification and Nomenclature of Enzymes

Enzymes are divided into 6 classes each with 4-13 subclasses and named accordingly by a four-digit number.

Oxidoreductases/dehydrogenases: Enzymes which catalyse oxidoreduction between two substrates S and S’.

Transferases: Enzymes catalysing a transfer of a group, G (other than hydrogen) between a pair of substrate S and S’.

Hydrolases: Enzymes catalysing hydrolysis of ester, ether, peptide, glycosidic, C-C, C-halide or P-N bonds.

Lyases: Enzymes that catalyse removal of groups from substrates by mechanisms other than hydrolysis leaving double bonds.

Isomerases: Includes all enzymes catalysing inter-conversion of optical, geometric or positional isomers.

Ligases: Enzymes catalysing the linking together of 2 compounds, e.g., enzymes which catalyse joining of C-O, C-S, C-N, P-O etc. bonds.

Co-factors

In many cases, non-protein constituents are bound to the enzyme which makes the enzyme catalytically inactive. Such non-protein constituents are called cofactors. In such cases, the protein portion of the enzyme is called the apoenzyme. There are three kinds of cofactors, viz. prosthetic groups, co-enzymes and metal ions.

Prosthetic Groups:

Prosthetic groups are organic compounds. They are distinguished from other cofactors in that they are tightly bound to the apoenzyme. For example, in peroxidase and catalase, which catalyze the breakdown of hydrogen peroxide to water and oxygen, haem is the prosthetic group and it is a part of the active site of the enzyme.

Co-enzymes:

Co-enzymes are also organic compounds but their association with the apoenzyme is only transient. A co-enzyme’s association; with apoenzyme; usually occurs during the course of catalysis. Moreover, co-enzymes serve as co-factors in a number of different enzyme catalyzed reactions. The essential chemical components of many coenzymes are vitamins, e.g., coenzyme nicotinamide adenine dinucleotide (NAD) and NADP contain the vitamin niacin.

Metal Ions: A number of enzymes require metal ions for their activity. Such metal ions form coordination bonds with side chains at the active site and at the same time form one or more cordination bonds with the substrate, e.g., zinc is a cofactor for the proteolytic enzyme carboxypeptidase. Catalytic activity is lost when the co-factor is removed from the enzyme which proves that they play a crucial role in the catalytic activity of the enzyme.

NCERT Solution for Class 11 Biology Biomolecules 

Question – 1 - What are macromolecules? Give examples.

Answer: Biomolecules with molecular weights more than one thousand Dalton are called biomacromolecules. These are found in the acid-insoluble fraction. Examples: Protein, polysaccharides, lipids, etc.

Question – 2 - Illustrate a glycosidic, peptide and a phospho-diester bond.

Answer:

Question – 3 - What is meant by tertiary structure of proteins?

Answer: The overall shape of a protein molecule; and the spatial relationship of the secondary structures to one another; is called tertiary structure of protein. In other words, the various folds which give three dimensional appearances to protein form its tertiary structure.

Question – 4 - Find and write down structures of 10 interesting small molecular weight biomolecules. Find if there is any industry which manufactures the compounds by isolation. Find out who are the buyers.

Answer:

Fat is manufactured by isolation. Many hormones are also manufactured by isolation. Pharmaceutical and consumer goods industry can be the major buyers of these products.

Question – 5 - Proteins have primary structure. If you are given a method to know which amino acid is at either of the two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?

Answer: If the same amino acid is present at both ends of protein, then it is a homopolymer. The protein is not pure in that case. On the other hand, a heteropolymer is a pure protein.

Question – 6 - Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins (e.g., Cosmetics etc.)

Answer: Contraceptive pills are hormones and hence are proteins. Additionally, there are many protein supplements available in the market. Collagen is a protein which is used as an additive in various food and cosmetics.

Question – 7 - Explain the composition of triglyceride.

Answer: When fatty acids are found esterified with glycerol, they are called glycerides. Presence of three esterified bonds makes them triglycerides.

Fig: An unsaturated fat Triglyceride

In this figure, the left side is composed of glyceride. The right side is composed of palmitic acid, ocleic acid and alpha-linolenic acid; from top to bottom.

Question – 8 - Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins?

Answer: Nearly 80% of milk protein is casein. Proteases act on the soluble portion of casein, i.e. K-casein. These leads to coagulation of milk protein and curd is formed.

Question – 9 - Attempt titrating an amino acid against a weak base and discover the number of dissociating ( ionizable ) functional groups in the amino acid.

Answer: When amino acid is titrated against a weak base, it ionizes into NH2 (amine group) and COOH (carboxylic group).

Question – 10 - Draw the structure of the amino acid, alanine.

Answer:

Fig: Alanine

Question – 11 - What are gums made of? Is Fevicol different?

Answer: Natural gum is a polysaccharide of natural origin. It has high viscosity even at low concentration. Fevicol is a synthetic glue. Synthetic glue is usually made of polymers which are dissolved in a solvent. When the adhesive is exposed, the solvent evaporates; resulting in hardening of the adhesive. Synthetic adhesives come in various strengths and are used accordingly.

Question – 12 - Find out a qualitative test for proteins, fats and oils, amino acids and test any fruit juice, saliva, sweat and urine for them.

Answer: Qualitative tests for proteins, fats and oils are as follows:

Biuret Test: Biuret test is done for protein. Appearance of violet colour in the solution confirms the presence of protein. Biuret (H2NCONHCONH2) reacts with copper ion in a basic solution and gives the violet colour.

Liebermann-Burchard Test: This test is done for cholesterol. The reagent is a mixture of acetic anhydride and sulphuric acid. Appearance of green colour confirms the presence of cholesterol.

Grease Test: This test is done for certain oils. This is a simple test which involves rubbing the given sample on cloth or paper. Appearance of a translucent spot shows the presence of oil.

Question – 13 - Find out how much cellulose is made by all the plants in the biosphere and compare it with how much of paper is manufactured by man and hence what is the consumption of plant material by man annually. What a loss of vegetation!

Answer: As per a UN report of 2006, about 312 million tons of carbon is stored as biomass of plants. About 10% of the total available cellulose is used in paper making. This appears as a small figure; compared to the total biomass. But when the lost forest cover is replaced by monoculture plantations, it makes the situation grim. Moreover, wood is also cut for many other purposes. Hence, there is a huge loss of vegetation every year.

Question – 14 - Describe the important properties of enzymes.

Answer: Enzymes are biological catalysts. No metabolic reaction takes place without an enzyme. Enzymes are highly specific to the substrates. Unlike inorganic catalysts, enzymes are susceptible to high temperatures and cease

Important Questions for NCERT Class 11 Biology Biomolecules

Ques. Macromolecule chitin is
(a) sulphur containing polysaccharide
(b) simple polysaccharide
(c) nitrogen containing polysaccharide
(d) phosphorus containing polysaccharide.

Answer: C

Ques. Carbohydrates are commonly found as starch in plants storage organs. Which of the following five properties of starch (1-5) make it useful as a storage material?
(1) Easily translocated
(2) Chemically non-reactive
(3) Easily digested by animals
(4) Osmotically inactive
(5) Synthesized during photosynthesis
The useful properties are
(a) (1), (3) and (5)    (b) (1) and (5)
(c) (2) and (3)          (d) (2) and (4). 

Answer: D

Ques. Cellulose is the major component of cell walls of
(a) Pseudomonas (b) Saccharomyces
(c) Pythium (d) Xanthomonas.

Answer: C

Ques. Carbohydrates, the most abundant biomolecule on earth, are produced by
(a) some bacteria, algae and green plant cells
(b) fungi, algae and green plant cells
(c) all bacteria, fungi and algae
(d) viruses, fungi and bacteria. 

Answer: A

Ques. Which of the following is a reducing sugar?
(a) Galactose (b) Gluconic acid
(c) β-methyl galactoside
(d) Sucrose 

Answer: A

Ques. Cellulose, the most important constituent of plant cell wall is made up of
(a) branched chain of glucose molecules linked by β-1, 4 glycosidic bond in straight chain and α-1, 6 glycosidic bond at the site of branching
(b) unbranched chain of glucose molecules linked by β-1, 4 glycosidic bond
(c) branched chain of glucose molecules linked by α-1, 6 glycosidic bond at the site of branching
(d) unbranched chain of glucose molecules linked by α-1, 4 glycosidic bond. 

Answer: B

Ques. Lactose is composed of
(a) glucose + galactose (b) fructose + galactose
(c) glucose + fructose (d) glucose + glucose.

Answer: A

Ques. In which of the following groups are all polysaccharides?
(a) Sucrose, glucose and fructose
(b) Maltose, lactose and fructose
(c) Glycogen, sucrose and maltose
(d) Glycogen, cellulose and starch 

Answer: D

Ques. Glycogen is a polymer of
(a) galactose (b) glucose
(c) fructose (d) sucrose. 

Answer: B

Ques. Which of the following are not polymeric?
(a) Proteins (b) Polysaccharides
(c) Lipids (d) Nucleic acids

Answer: C

Ques. Nucleotides are building blocks of nucleic acids. Each nucleotide is a composite molecule formed by
(a) base-sugar-phosphate
(b) base-sugar-OH
(c) (base-sugar-phosphate)n
(d) sugar-phosphate. 

Answer: A

Ques. Which purine base is found in RNA?
(a) Thymine (b) Uracil
(c) Cytosine (d) Guanine 

Answer: D

Ques. Which of the following nucleotide sequences contains 4 pyrimidine bases?
(a) GATCAATGC (b) GCUAGACAA
(c) UAGCGGUAA (d) Both (b) and (c)

Answer: A

Ques. In RNA, thymine is replaced by
(a) adenine (b) guanine
(c) cytosine (d) uracil. 

Answer: D

Ques. Adenine is
(a) purine (b) pyrimidine
(c) nucleoside (d) nucleotide. 

Answer: A

Ques. A nucleotide is formed of
(a) purine, pyrimidine and phosphate
(b) purine, sugar and phosphate
(c) nitrogen base, sugar and phosphate
(d) pyrimidine, sugar and phosphate. 

Answer: C

Ques. DNA is composed of repeating units of
(a) ribonucleosides
(b) deoxyribonucleosides
(c) ribonucleotides
(d) deoxyribonucleotides. 

Answer: D

Ques. The basic unit of nucleic acid is
(a) pentose sugar (b) nucleoid
(c) nucleoside (d) nucleotide. 

Answer: D

Ques. RNA does not possess
(a) uracil (b) thymine
(c) adenine (d) cytosine. 

Answer: B

Ques. “Ramachandran plot” is used to confirm the structure of
(a) RNA (b) proteins
(c) triacylglycerides (d) DNA.

Answer: B

Ques. Which of the following is the least likely to be involved in stabilising the three-dimensional folding of most proteins?
(a) Hydrogen bonds
(b) Electrostatic interaction
(c) Hydrophobic interaction
(d) Ester bonds

Answer: D

Ques. Identify the substances having glycosidic bond and peptide bond, respectively in their structure.
(a) Chitin, cholesterol (b) Glycerol, trypsin
(c) Cellulose, lecithin (d) Inulin, insulin

Answer: D

Ques. Which of the following biomolecules does have a phosphodiester bond?
(a) Amino acids in a polypeptide
(b) Nucleic acids in a nucleotide
(c) Fatty acids in a diglyceride
(d) Monosaccharides in a polysaccharide 

Answer: B

Ques. Which is wrong about nucleic acids?
(a) DNA is single stranded in some viruses.
(b) RNA is double stranded occasionally.
(c) Length of one helix is 45 Å in B-DNA.
(d) One turn of Z-DNA has 12 bases. 

Answer: C

Ques. A segment of DNA has 120 adenine and 120 cytosine bases. The total number of nucleotides present in the segment is
(a) 120 (b) 240
(c) 60 (d) 480. 

Answer: D

Ques. Which is not consistent with double helical structure of DNA?
(a) A = T, C = G
(b) Density of DNA decreases on heating.
(c) A + T/C + G is not constant.
(d) Both (a) and (b) 

Answer: C

Ques. In double helix of DNA, the two DNA strands are
(a) coiled around a common axis
(b) coiled around each other
(c) coiled differently
(d) coiled over protein sheath.

Answer: A