NCERT Solutions for Class 11 Biology Chapter 9 Biomolecules are provided here with simple step-by-step explanations. These NCERT solutions for Biomolecules are extremely popular among class 11 medical students for Biology. NCERT Solutions for Class 11 Biology Chapter 9 Biomolecules are important concepts in understanding the chemical composition of matter found in living entities. This chapter is categorised under the latest CBSE Syllabus.
Biomolecules NCERT Solutions come handy for quickly completing your homework and preparing for CBSE board exams. All questions and answers from the NCERT Book of class 11 Biology Chapter 9 are provided here for you for free. All NCERT Solutions for class 11 Biology are prepared by experts of ANAND CLASSES and are 100% accurate.
Students who look forward to making a career in the medical field must know the fundamentals of Biology Subject. NCERT Solutions for Class 11 chapter 9 include solved solutions for all the questions appearing in the textbook, answered in the same order for the convenience of students.
NCERT Solutions for Class 11 Biology Chapter 9 – Biomolecules
What are Macromolecules? Give examples.
“Macromolecules are very large molecules that are formed by the polymerization of large number of micromolecules called monomers and possessing higher molecular weight.” Macromolecules are polymers with a molecular mass of 10,000 daltons or more.
Micromolecules are found in the colloidal state in the intercellular fluid due to their insoluble nature.
Therefore, macromolecules are large complex molecules that occur in colloidal state in intercellular fluid.
Examples : Polysaccharides, proteins, and nucleic acids are common examples of macromolecules.
Illustrate a glycosidic, peptide and a phospho-diester bond.
A Glycosidic bond is a type of covalent bond formed between the aldehyde or ketone group of one carbohydrate (sugar) molecule and the hydroxyl group of another carbohydrate (sugar) molecule is called a glycosidic bond.
The bond between the individual monosaccharides is called a glycosidic linkage. This bond is formed between two carbon atoms of two adjacent monosaccharide units.
- When two sugar molecules are joined by a glycosidic bond it forms a disaccharide
- Several sugar molecules are linked together and are known as oligosaccharides.
- And when a long chain of sugar molecules is linked it is called a polysaccharide. Therefore, they are important for the formation of oligosaccharides and polysaccharides.
Hence, a Glycosidic bond :
- It is a type of covalent bond.
- Formed between anomeric carbon and alkoxy oxygen of sugar molecules.
- When two or more sugar molecules (monosaccharides) are joined by glycosidic bonds it forms disaccharide and polysaccharides respectively.
- Thus, this is the type of bond that occurs between sugar molecules.
For example, Sucrose, cellulose, and maltose are formed by the joining of two or more monosaccharide units.
Following figure shows Sucrose is formed when a monomer of glucose and a monomer of fructose are joined in a dehydration/condensation reaction to form a glycosidic bond between carbon 1 in glucose and carbon 2 in fructose. In the process, a water molecule is lost.
During the formation, there is a removal of water molecules hence, this is a condensation process. Condensation takes place between a hydroxyl oxygen atom on carbon in one sugar and the anomeric carbon of another sugar.
When the alcohol group attacks the anomeric carbon, the OH group which is bound to that carbon is replaced by the oxygen of alcohol and it eliminates the hydrogen of alcohol. Therefore, there is the removal of OH and H in the form of water.
A peptide bond is a covalent bond that is formed when the alpha carboxyl group (-COOH) of one amino acid (C-terminal) chemically react with the alpha amino group (-NH2 ) of the adjacent amino acid (N-terminal) and an amide bond (CO−NH) or peptide bond is formed with the releasing a water molecule and forms a protein (resulting in a peptide chain.).
This reaction is known as dehydration synthesis/condensation. The newly formed amino acids are also called a dipeptide.
Peptide is a Greek word that means “digested”. A peptide is a short polymer of amino acid monomers linked by an amide bond. A peptide bond, also called an eupeptide bond.
Peptide Bond in Protein
A peptide consists of a chain of many amino acids. On the contrary, a protein contains a long chain of peptides with 50 or more amino acids. Therefore, proteins are long chains of amino acids held together by peptide bonds. Not all peptides form proteins, but all proteins consist of peptides. Typically, proteins display a more complex structure than simpler peptides.
The presence of proteins in a substance can be detected using a test called the Biuret test.
Explain the mechanism of Peptide bond formation
- The mechanism of peptide bond formation is a dehydration synthesis process.
- During the formation of a peptide bond, the carboxyl group of one amino acid moves towards the amino group of another amino acid.
- Subsequently, one hydrogen and one oxygen atoms are lost from the carboxyl group (COOH) of the first amino acid. In contrast, one hydrogen is lost from the amino group (NH2) of the other amino acid.
- This results in the release of a water molecule (H2O) along with the formation of an amide bond (-NH-C=O) between the two amino acids.
- The process of formation of a peptide bond between two amino acids results in a dipeptide molecule.
- Thus, a peptide bond is formed when the carboxyl group of one amino acid condenses with the amino group of another amino acid releasing in a water molecule.
- The formation of the peptide bond is an endergonic reaction that requires energy, which is obtained from ATP in living beings.
- Because this reaction involves the removal of a water molecule, it is called a dehydration synthesis reaction.
What are the important characteristics of Peptide Bond in a Polypeptide ?
- It connects two amino acid groups through dehydration synthesis.
- A partial double bond exists between carbon and nitrogen of the amide bond which stabilizes the peptide bond. They are not broken by heating or high salt concentration.
- Peptide bond is strong, kinetically stable, and requires high activation energy to break the bond. Only a long-time exposure to strong acid or base at an elevated temperature can break it. Some specific enzymes, like digestive enzymes, can result in the cleavage.
- The peptides are rigid and planar, which means that the C=O and the N-H bonds lie on the same plane, and the rotation about the peptide bond is restricted. The lack of rotation allows the peptide group to remain fixed in either a cis or trans configuration (stereochemistry), thereby stabilizing protein structure.
- Trans configuration of the peptide group allows less steric hindrances of adjacent amino acid side chains.
- The N-H and C=O bonds are polar, i.e., partially positive H and partially negative O. Hence, different regions of the peptide can form hydrogen bonding.
- The number of amino acids in a peptide can range from two amino acids to fifty amino acids.
- Based on the number of amino acids present in the peptide, peptides are of many types; peptides with ten or fewer amino acids are termed oligopeptides, and the peptides with more than ten amino acids are termed polypeptides.
- Polypeptides with around 100 amino acids are then considered proteins.
What is the Importance of Peptide Bond ?”
The peptide bond is one of the essential biochemistry reactions since it is used by amino acids to form proteins. The function of a peptide bond is to maintain the stability of proteins. In living organisms, proteins are used in many roles. These include physical support, catalyzing energetic reactions, and identifying molecules in the environment. The peptide bond is essentially the basis of many biological reactions. The formation of peptide bonds is a requirement for all life. This forming is very similar in all forms of life.
What are the Different Forms of Peptide Bond ?
The peptide bond is present in all proteins that bind the amino acid in the chain together.
- Monopeptide: having one amino acid
- Dipeptide: having two amino acids
- Tripeptide: having three amino acids
- Tetrapeptide: having four amino acids
- Pentapeptide: having five amino acids
- Hexapeptide: having six amino acids
- Heptapeptide: having seven amino acids
- Octapeptide: having eight amino acids
- Oligopeptide = contains not more than 10 amino acid units.
- Polypeptide = contains more than 10 amino acid units, up to 100 residues.
- Macropeptides = made up of more than 100 amino acids.
Explain the Peptide bond degradation mechanism
As a result of its resonance stabilization, a peptide bond is almost unreactive under physiological conditions.
- The degradation of the peptide bond takes place through hydrolysis, thus requires the presence of water molecules.
- The degradation reaction is very slow as the amide bond between the amino acids is stabilized by the partial double bond.
- Because of the partial double bond between carbon and nitrogen molecule, carbon atom generates a slight positive charge.
- In the presence of water, the OH– ions of water attack the carbon atom, which results in degradation of the peptide bond.
- The remaining hydrogen ion of the water then attacks the nitrogen atom resulting in the amino group.
- As a result of this, the peptide molecule is cleaved into two units; one unit with the carboxyl group and another with the amino group.
The degradation of the peptide is an exergonic reaction that releases about 8-16 kj/mole of energy.
Because the protein degradation reactions are very slow, they are usually catalyzed by proteolytic enzymes like proteases and peptidases.
Explain the Peptide bond hydrolysis process
Peptide bond hydrolysis is the primary step of all protein hydrolysis reactions.
The most common method of protein degradation is acid-catalyzed hydrolysis of the peptide bond.
Peptide hydrolysis is also essential in some synthetic reactions where amino acids in one peptide are cleaved and transferred to another peptide, resulting in separate peptide synthesis.
Similarly, different peptides and proteins accumulate in cells resulting in toxicity. Peptide bond hydrolysis is essential in the removal of those toxins as well.
Peptide bond hydrolysis is also an important step in the digestion of proteins in living beings.
Hydrolysis of peptide bond occurs in the presence of water and is catalyzed by the presence of acid.
Peptide bond hydrolysis is one of the mechanisms of peptide bond degradation where polypeptides are either cleaved into smaller peptides, or smaller peptides are degraded into separate amino acids.
Acid-catalyzed hydrolysis of the peptide bond is as follows :
Note in the above chemical equation, positive ions made from the -NH2 groups reacting with hydrogen ions.
You need the extra hydrogen ion in the equation (compared with the amide equation) to react with the -NH2 group on the left-hand end of the dipeptide – the one not involved in the peptide link.
If you scale this up to a polypeptide (a protein chain), each of the peptide links will be broken in exactly the same way.
That means that you will end up with a mixture of the amino acids that made up the protein – although in the form of their positive ions because of the presence of the hydrogen ions from the hydrochloric acid.
Explain the Peptide Bond Resonance Structure
The general structure of the peptide group is rigid, trans and planar. The coplanarity of the peptide bond denotes the resonance or partial sharing of two pairs of electrons between the amide nitrogen and carboxyl oxygen.
The Peptide Bond Resonance Structure is as follows :
The atoms C, H, N, and O of the peptide bond lie in the same plane, like the hydrogen atom of the amide group and the oxygen atom of the carboxyl group, which are trans to each other.
Linus Pauling and Robert Corey are the scientists who found that the peptide bonds are rigid and planar.
Stability of a peptide bond
The stability of a peptide bond is because of the resonance of the amide. A resonance structure forms due to the interaction between electrons of the carbonyl group’s double bond with those of the C–N bond. This effect is an example of resonance, which can be considered to share electrons between bonds. As a result, the C-N acquires a partial double bond property. The C=O bond acquires a partial single bond property.
Since single bonds between two atoms are longer than double bonds between the same two atoms, the lengths of the C–N and C=O bonds in a peptide differ from those observed in structures without resonance. Thus, the partial double bond character of C–N implies that this bond is shorter than would be predicted for a regular C–N single bond. On the other hand, the C=O bond is more extended than predicted for a regular C=O double bond.
What is the rule to naming of the Peptide Bond ?
The peptide or protein of the amino acid is represented by the 3 letters or one-letter abbreviation. To name the peptides, we should know the suffixes of the amino acids. -ine for glycine, -an for tryptophan, -ate for glutamate, are changed to -yl, except in the case of the C-terminal of the amino acid.
Peptide Bond Examples
A simple example of a peptide is the dipeptide called glycylglycine. It is formed from glycine residues. Other examples are as follows :
Phosphodiester bonds are the backbone of the strands of nucleic acid present in the life existing on Earth.
Phosphodiester bonds are formed due to the reaction in between the hydroxyl groups of two sugar groups and a phosphate group and thus, oligonucleotide polymers are formed as the result of a combination of the diester bond in the phosphoric acid and the sugar molecules present in the DNA and RNA backbone. Phosphodiester bond is responsible for holding the backbone of DNA and RNA in an animal body.
The phosphodiester bonds are formed as the result of the condensation reaction between phosphate groups and hydroxyl groups of two sugar groups.
Phospho-diester bond joins successive sugar molecules in a polynucleotide. It is a strong covalent bond formed between two adjacent sugar groups and phosphate. These are the bonds that form the sugar-phosphate backbone of the nucleic acids.
What is meant by the tertiary structure of proteins?
The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space.
The secondary structure of a protein can be further folded or coiled into a tertiary structure. The tertiary structure is made up by different combinations of alpha helices and beta pleated sheets.
The tertiary structure is primarily due to interactions between the R groups of the amino acids that make up the protein.
The tertiary structure involves four types of bonds:
- Ionic bonds
- Disulfide bridges
- Hydrophobic forces
- Hydrogen bonds
Ionic bonds contribute to folding
Ionic bonds result from the electrostatic interactions between electrochemically charged side-chains of different amino acids. These bonds contribute to the folding process of the tertiary structure.
Disulfide bonds (S – S)
Disulfide bonds are covalent bonds which form between cysteine residues, are much stronger than the other types of bonds that contribute to tertiary structure. They act like molecular “safety pins,” keeping parts of the polypeptide firmly attached to one another.
Cysteine is the only amino acid that contains sulfur containing sulfhydryl groups (-SH). When in close proximity to another cysteine, the sulfur atom of one cysteine can covalently bond with a sulfur atom of the neighbouring cysteine to produce a disulfide bond, which is a covalent bond and is very important for the structure of proteins.
Also important to tertiary structure are hydrophobic interactions, in which amino acids with nonpolar, hydrophobic R groups cluster together on the inside of the protein, leaving hydrophilic amino acids on the outside to interact with surrounding water molecules.
Hydrophobic (non-polar) amino acids, such as valine and proline, are ‘repelled’ from water. Therefore they get pushed “inside” the protein due to water molecules in their environment. Hydrophobic Forces occur between non-polar amino acids.
Hydrogen bonds between the polar, charged amino acids contribute to the tertiary structure. These are all weak interactions in the cellular environment, but their cumulative effect helps give proteins their unique shape. The hydrogen bonds between the amino acids help to maintain the shape of the protein, and prevent it from falling apart or denaturing.
Proteins consisting of only one polypeptide chain have their tertiary structure as their final structure.
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.
Proteins have a 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 the purity or homogeneity of a protein?
The primary structure of a protein is defined as the sequence of amino acids linked together to form a polypeptide chain. Each amino acid is linked to the next amino acid through peptide bonds created during the protein biosynthesis process. This positional information of a protein is called the primary structure of the protein. The first amino acid in a protein is called the N-terminal amino acid, and the last amino acid in a protein is called the C-terminal amino acid.
Yes, if we are given a method to know the sequence of proteins, we can connect this information to the purity or homogeneity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. If we are provided with a method to know the sequence of an unknown protein, then using this information, we can determine its structure and compare it with any of the known correct protein sequences. Any change in the sequence can be linked to the purity or homogeneity of a protein.
For example, anyone change in the sequence of haemoglobin can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.
Also on the basis of carboxyl and amino groups, amino acids can be acidic, basic and neutral. Proteins can be acidic, basic and neutral.
Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins (e.g., Cosmetics, etc.)
Proteins are very essential for the structural and functional growth of the body. Proteins and peptides are widely used as pharmaceutical agents in antiviral agents, antibiotic, as prodrug and even antimicrobial agent.
Following is the list of proteins used as therapeutic agents.
Proteins with therapeutic uses are Insulin, Oxytocin, Immunoglobin, Antidiuretic Hormone( ADH), Thrombin, Fibrinogen, Renin, diastase and streptokinases etc
Some other applications of proteins are :
As cosmetics – Protein such as casein is used in beauty creams, shampoos, etc.
Sweeteners – They are used as artificial sweeteners. Thaumatin and monellin is a low-calorie sweetener.
Dietary supplements – Proteins are used as dietary supplements to maintain health.
Explain the composition of triglyceride.
Triglycerides are a type of fat (lipid) found in your blood. When you eat, your body converts any calories it doesn’t need to use right away into triglycerides. The triglycerides are stored in your fat cells. Later, hormones release triglycerides for energy between meals
Triglyceride, an ester derived when glycerol combines with three fatty acids on each of the OH groups through ester bonds, it is known as a triglyceride.
All three fatty acids of triglyceride in pure fat are similar (n tripalmitin), while in mixed fat, they are dissimilar (palmetto-oleostearin, dipalmitostearin).
Glycerol is a triol, an alcohol which contains three hydroxyl functional groups. A fatty acid is a long carbon chain, generally 12 to 24 carbons in length, with an attached carboxyl group. Each of the three fatty acid molecules undergoes an esterification with one of the hydroxyl groups of the glycerol molecule. The result is a large triester molecule referred to as a triglyceride.
Triglycerides function as a long-term storage form of energy in the human body. Because of the long carbon chains, triglycerides are nearly nonpolar molecules and thus do not dissolve readily in polar solvents such as water. Instead, oils and fats are soluble in nonpolar organic solvents such as hexane and ethers.
Fats may be either saturated or unsaturated. A saturated fat is a fat that consists of triglycerides whose carbon chains consist entirely of carbon-carbon single bonds. Therefore, the carbon chains are saturated with the maximum number of hydrogen atoms possible. An unsaturated fat is a fat that consists of triglycerides whose carbon chains contain one or more carbon-carbon double bonds. A fat with one double bond is called monounsaturated, while a fat with multiple double bonds is called polyunsaturated (see figure below).
High consumption of saturated fats is linked to an increased risk of cardiovascular disease. Some examples of foods with high concentrations of saturated fats include butter, cheese, lard, and some fatty meats. Foods with higher concentrations of unsaturated fats include nuts, avocado, and vegetable oils such as canola oil and olive oil.
Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins
Milk contains a protein called casein. When we add a little amount of curd to the milk, the milk protein casein gets is denatured, which transforms globular proteins into fibrous proteins and coagulated due to the action of lactic acid bacteria, and as a result, the milk is converted into curd or yoghurt. Coagulation disrupts the structure of the protein casein.
Can you attempt building models of biomolecules using commercially available atomic models (Ball and Stick models)?
Yes, we can attempt to build models of biomolecules using commercially available atomic models such as ball and stick models. In these models, the stick is assumed to be a bond which hold the molecule, while balls of different colours are assumed to be atoms.
The figure above is a model of amino acid, where atoms of hydrogen are indicated by blue balls, oxygen atoms are represented by red balls, and carbon atoms are represented by grey balls.
Attempt titrating an amino acid against a weak base and discover the number of dissociating (ionisable) functional groups in the amino acid.
When we titrate an amino acid against a weak base, it dissociates into its functional groups, i.e. -COOH (carboxylic group) and -NH2 (amino group). The pH of the amino acid is recorded, and the weak base is slowly supplemented to the amino acids while continuously noting the pH. The number of changes recorded indicates the number of ionisable functional groups –COOH in the acidic range and –NH2 in the alkaline range.
Draw the structure of the amino acid alanine.
The structure of Alanine is as follows:
What are gums made of? Is Fevicol different?
Gums are heteropolysaccharides made of various monosaccharide units linked together by glycosidic bonds. However, because Fevicol is composed of synthetic polymers, it differs from gums.
Find out a qualitative test for proteins, fats and oils, and amino acids and test any fruit juice, saliva, sweat and urine for them.
Qualitative test for proteins
Xanthoproteic test : Xanthoproteic test identifies when urine is tested for protein with the help of the xanthoproteic test, the presence of a yellow precipitate confirms the presence of protein in it.
Biuret test : Biuret test identifies the presence of proteins by turning the colour of the solution from light blue to purple.
Qualitative test for fats and oils
Emulsification test : The qualitative test for fats is the emulsification test. In this test, the experimental material is treated with ethanol and then dissolved in water. The formation of emulsion confirms the presence of fats.
Paper test : The qualitative test for oils is the paper test. The experimental material is put on paper. If oil marks are left, the presence of oil is confirmed.
Qualitative test for amino acids
Ninhydrin test : Upon adding ninhydrin reagent to the solution, the colour of the solution turns to pink, purple or blue based on the type of amino acid.
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!
Paper is made up of pulp from wood, which is mainly composed of cellulose. Cellulose is a polymer of glucose molecules joined together. The biosphere produces about 100 billion tonnes of cellulose out of 170 billion tonnes of total organic matter. Paper manufacturing consumes 0.5 billion tonnes of wood. The increase in consumption of wood has led to a great loss of vegetation.
Describe the important properties of enzymes.
Enzymes are proteinaceous substances that are capable of catalysing chemical reactions of biological origin without themselves undergoing any change. They are commonly called as biocatalysts. The properties of enzymes are as follows:
- Enzymes are proteins by nature
- They have a higher molecular weight and are complex macromolecules.
- They catalyse the biochemical reactions involved in the cell, assisting in breaking down larger molecules into simpler molecules or getting together two smaller molecules to form a larger one.
- Enzymes do not initiate but accelerate a reaction.
- They affect the rate of biochemical reaction and do not influence the direction of the reaction.
- They are action-specific.
- A higher turnover of enzymes causes an increase in the efficiency of a reaction. Most of the enzymes have a high turnover number.
- Optimum temperature – Enzymes are affected by temperature. As the temperature increases, enzymatic activity decreases. Maximum activity is observed at 30-40 degree Celsius. An enzyme is active within a narrow range of temperatures. The temperature at which an enzyme is most active is called the optimum temperature. The enzyme activity decreased above and below this temperature
- Optimum pH : Every enzyme has an optimum pH at which it is most active. Most of the intracellular enzymes work at a neutral pH. Maximum activity is observed at a 6-8 pH level.
- Enzymes are substrate specific i.e. one enzyme catalyses only a particular substrate. Every enzyme has specific sites called active sites for the binding of substrate. With an increase in substrate concentration, the enzymatic velocity also increases, reaching maximum velocity.
- Only a small quantity of enzyme is capable of forming the desired product.
- Enzyme activity is sensitive to certain chemicals called inhibitors or modulators
NCERT Solutions for Class 11 Biology Chapter 9 – Biomolecules
NCERT Solutions for Class 11 Biology Chapter 9 – Biomolecules are categorised under Unit 3 – Cell: Structure and Functions of the latest CBSE Syllabus. This particular unit totals up to 15 marks as per the previous years’ question papers which approximately adds up to 21% of the total weightage of the paper.
Students can revise from previous years’ question papers to get an idea of the typology of questions that can be expected from this chapter. Apart from learning concepts, knowing how to answer is the key to scoring optimum marks, and NCERT Solutions help students with it.
List of subtopics covered in Chapter 9 – Biomolecules
|How to analyse chemical composition?
|Primary and Secondary Metabolites
|Structure of Proteins
|Nature of Bond Linking Monomers in a Polymer
|Dynamic State of Body Constituents – Concept of Metabolism
|Metabolic Basis for Living
|The Living State
NCERT Solutions for Class 11 Biology Chapter 9 – Biomolecules
Biomolecules include some important topics which enable students to understand the chemical composition. To be able to analyse a living tissue sample and identify a specific organic compound in higher classes, a fundamental understanding of different types of tissues, anatomy, morphology, the common site at which they are found, different functionalities they carry out, etc., are equally required to comprehend concepts.
Students thus understand different chemical reactions and their conversions, the role of enzymes, the nature of different enzyme actions, various factors affecting the activity of enzymes, and the classification and nomenclature of different enzymes.
Key Features of NCERT Solutions for Class 11 Biology Chapter 9 – Biomolecules
- Solutions framed by subject-matter experts.
- Solutions are provided as per the expected answering pattern.
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Frequently Asked Questions on NCERT Solutions for Class 11 Biology Chapter 9
List out the properties of enzymes covered in Chapter 9 of NCERT Solutions for Class 11 Biology.
The properties of enzymes covered in Chapter 9 of NCERT Solutions for Class 11 Biology are
- The enzymes have higher molecular weight and are complex macromolecules.
- The biochemical reactions involved in the cell are catalysed by the enzymes, assisting in breaking down larger molecules into simpler molecules.
- Enzymes only accelerate a reaction.
- The rate of biochemical reaction is affected by the enzymes and does not influence the direction of the reaction.
- Enzymes are action specific.
- The maximum activity of enzymes is observed at a 6-8 pH level.
What are the fundamental concepts I can learn from Chapter 9 of NCERT Solutions for Class 11 Biology?
The fundamental concepts you can learn from Chapter 9 of NCERT Solutions for Class 11 Biology are
9.1 – How to analyse chemical composition?
9.2 – Primary and Secondary Metabolites
9.3 – Biomacromolecules
9.4 – Proteins
9.5 – Polysaccharides
9.6 – Nucleic Acids
9.7 – Structure of Proteins
9.8 – Nature of Bond Linking Monomers in a Polymer
9.9 – Dynamic State of Body Constituents – Concept of Metabolism
9.10 – Metabolic Basis for Living
9.11 – The Living State
9.12 – Enzymes
Why should students refer to the NCERT Solutions for Class 11 Biology Chapter 9?
- The NCERT Solutions are tailored by the subject-matter experts with utmost care.
- The faculty make use of step-wise answering patterns, which help students to score more marks in the board exam.
- PDF format solutions are available with a free download option.
- Effective and efficient reference tool which the students can rely on.
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