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CBSE Quick Revision Notes Class 11 Biology Chapter 9: The NCERT chapter 9 Biomolecules provide you with insight into the components of living organisms. The NCERT Class 11 Biology Chapter 9 notes cover a brief outline of the chapter biomolecules. The main topics covered in Biomolecules NCERT Class 11 Biology Notes are: definition of biomolecules, how to analyse the chemical composition, primary and secondary metabolites, biomacromolecules, carbohydrates, lipids, Nucleic Acids, proteins, monomers, Metabolic process, living state, enzyme, nature of enzyme activity, factors affecting enzymes, cofactors. Class 11 biology chapter 9 notes cover all the important concepts of this chapter in easy and simple language. Having revision notes and NCERT Solutions for Class 11 Biology Chapter 9 handy is crucial to saving you time. The NCERT Class 11 Biology chapter 9 notes PDF can be downloaded through the link given below.
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Biomolecules Class 11 notes Biology Chapter 9 also covers all the important headings of the NCERT Textbook that are useful in various competitive exams. Chapter 9 Biomolecules Notes help you revise these major concepts given in the NCERT Book in a short period of time during CBSE Board exam preparation. Download the CBSE Notes for Class 11 Biology Chapter 9 PDF to use them offline anywhere. They can be downloaded through the link. Students must go through each topic in Biomolecules Class 11 Notes Biology in the easiest and most effective way possible with the help of NCERT Notes for Class 11. Check the given Class 11 Biology Notes Chapter 9 Biomolecules PDF for quick revision. Biology Biomolecules notes will take you on a journey through the different types of biomolecules found on this earth.
Also, students can refer to:
This table depicts the comparison between elements present in living and nonliving matter.
Elements | % in Earth's crust | %in the Human body |
Hydrogen | 0.14 | 0.5 |
Carbon | 0.03 | 18.5 |
Oxygen | 46.6 | 65.0 |
Nitrogen | Very Little | 3.3 |
Sulphur | 0.03 | 0.3 |
Sodium | 2.8 | 0.2 |
Calcium | 3.6 | 1.5 |
Magnesium | 2.1 | 0.1 |
Silicon | 27.7 | Negligible |
Trichloroacetic acid is used to fractionate Biomolecules. We get 2 fractions after treatment.
Acid soluble fraction:- In the filtrate
Contain all micro molecules except lipids.
Acid insoluble fraction
Contain macromolecular and lipids.
Primary Metabolites - These are the metabolites that have direct involvement in growth, development, and reproduction.
Example:- Amino acid
Secondary Metabolite - They are not directly involved in growth and development.
Example:- Alkaloids, Toxins, Drugs
Biomacromolecules:- Compounds having a molecular weight of less than 1000 dalton are called biomacromolecules.
Example:- Amino acid
Biomacromolecule: Compounds having a molecular weight of range of 10 thousand daltons ( except lipids ) are called biomacromolecules.
Example:- carbohydrates
It can be monosaccharides, oligosaccharides, polysaccharides
Monosaccharides | Oligosaccharides | Polysaccharides |
They are made up of a single unit. | They are made up of 2 -10 units. | They are made up of more than 10 units. |
Sweet in taste. | Sweet in taste. | Not sweet in taste. |
They are sugar. | They are sugar | They are non-sugar. |
Example - Triose - Glyceraldehyde Tetrose - erythrulose Pentose - Ribose ,xylose Hexose - Glucose, Fructose, galactose Heptose - sedoheptulose | Example- Disaccharides - Maltose, Lactose, Sucrose Trisaccharides - Raffinose Tetrasaccharides - Stachyose Pentasaccharide - Barbacos | Example - Starch -
Insulin
|
They are micromolecules that yield high energy.
It is of 3 types:-
Simple | Compound | Derived |
It includes: Triglycerides | It includes:- Phospholipids
| It includes:- Steroids
|
Monoglycerides - Monohydroxy alcohol + Fatty acid
| Glycolipids
| Terpenes
|
Cutin
| Chromolipids
| Prostaglandins
|
Suberin
| Lipoproteins
|
Triglycerides are composed of Glycerol + 3 Fatty acid
Fatty Acids are Further Classified As:
Saturated | Unsaturated |
CnH2nO is a general formula. n = number of carbon | CnH2n-2xO2 is a general formula. n = no of C x = no of the double bond |
n= 16 Palmitic Acid n= 18 Stearic Acid n= 20 Arachidic Acid | n =18 ,x=1 ,Oleic, Also called MUFA( mono unsaturated fatty acids) n= 18, x=2. , Linoleic n= 18,x =3, Linolenic |
Examples of Triglycerides are:-
Fat
It contains saturated fatty acid.
Remain solid at room temperature
Tripalmitin, Tristeric are examples of fat.
Oil
It contains unsaturated fatty acids.
Remain liquid at Room temperature.
Triolein , Gingelly seed are examples of oil
All amino acids are optically active except glycine.
They are small, colorless crystalline solids
They are soluble in water, insoluble in organic solvents. There are 20 amino acids.
Function
Glycine is the precursor of Haeme.
Tyrosine is the precursor of Thyroxine, Melanin
Tryptophan is the precursor of Niacin.
Some amino acids act as neurotransmitters. Eg: GABA
They are Heteropolymer.
2 Amino acids are linked by peptide bonds.
The most abundant protein in the animal world is Collagen.
Most abundant protein in the biosphere is - RUBISCO.
They are classified into 4 types on the basis of folding complexity.
Primary Structure | Secondary Structure | Tertiary Structure | Quaternary Structure |
|
|
| When different polypeptides with their own level arrange with respect to each other it gives rise to the quaternary structure. |
It tells us about the position of different amino acids in a chain. | It gives a 3D structure to a compound. | ||
Example:- Cysteine...Alanine...serine It is a hypothetical example of a primary chain. | Found in the keratin of skin, hair | Found in each chain of haemoglobin | Found in haemoglobin. All chains are connected together to form haemoglobin. |
Nitrogenous bases are of 2 type
Purine:- double-ringed
Example- Adenine, Guanine
Pyrimidine:- They are single-ringed.
Example:- Thymine, Uracil, cytosine
Ribose
Deoxyribose
Nucleoside= Sugar + Base
Nucleotide = Sugar + Base + phosphate
Examples of nucleic Acids are DNA, RNA
Double Helix Structure of DNA cis described by Watson and Crick.
Bases are attached to sugar N- glycosidic bond in 3' to 5' direction.( 3' C of nucleotide to 5'C of sugar)
Phosphates are attached to sugar by phosphodiester bonds.
Metabolism = Catabolism + Anabolism
Catabolic pathway - Pathways that lead to degradation of compounds.
Anabolic pathway - pathway which leads to the formation of compounds.
Term enzyme was given by Kuhne.
Enzymes are bio catalysts made up of protein ( exception -Ribozyme).
Enzymes are thermolabile..ie..they degrade at high temperature.
Enzymes are used to catalyse inorganic reactions.
Example:- Carbonic amylase accelerate the reaction by 10 million times
Enzymes have active sites..ie..sites for holding the substrate.
Then convert that substrate into a product by different transition states.
S - P
S ...> ES ....> P+ E Action of enzyme
S= substrate P= product
Enzymes lower the activation energy.
Maximum Binding energy is released due to maximum interaction between enzyme and substrate, which ultimately lowers the activation energy.
E = enzyme P = product
S = substrate
Substrate get bind to the active site of an enzyme to form ES complex
ES = enzyme-substrate complex
This binding leads to shape alteration of active sites.
E + S forms ES COMPLEX..and then EP complex
Then, enzymes get separated out leaving the product.
At optimum temperature, the enzyme shows maximum binding.
The optimum temperature of enzymes is 25°C - 40°C.
Enzyme activity varies with temperature as shown in the graph.
Each enzyme has its optimum ph for its maximum functioning.
Example:- pepsin has an optimum ph of 1.5 - 2.5
Trypsin has an optimum ph of 7.5 - 8.5
With the fixed molecules of an enzyme, the rate of reaction or velocity increases with the increase of substrate up to a particular limit.
Km value - It is the substrate concentration at which enzymes attain half of their max velocity.
Km is inversely proportional to the affinity of the enzyme with its substrate.
They are the structure resembling the substrate
Enzymes are sensitive to these inhibitors, thus they affect binding.
They are of many kinds: Example; Competitive inhibitors, non-competitive inhibitors, Allosteric inhibitors
Enzyme commission has developed a rule for naming enzymes.
Enzymes are classified according to the chemical reaction it catalyses.
EC numbers are 4-digit numbers given to each enzyme.
1st no. denote - major class
2 nd number denote- sub class
3 rd no. denote - sub sub class
4 th no. denotes - the serial number in sub sub class .
The first number, denoting class can be classified into 6 groups
EC1
OXIDOREDUCTASE
Example- oxidases, oxygenases
EC2
TRANSFERASES
Example:- Kinases
EC3
HYDROLASES
Example - Peptidases
EC4
LYASES
Example - Aldolases
EC5
ISOMERASES
Example - Mutase
EC-6
LIGASES
Example- Carboxylases
Enzymes are of 2 type
Simple
Conjugate
The Conjugate Enzyme Has 2 Parts:
Protein part called Apoenzyme
Non-protein part called Cofactors. These cofactors can be organic and loosely bound called Coenzyme.
Example- NAD has vitamin niacin
Cofactors that are organic and tightly bound are called a prosthetic group.
Eg- Haeme in peroxidase.
NCERT Class 11 chapter 9 Biomolecules contains the overview of element founds in different living organisms and their function. Also what is the availability of that elements in non livings and their functions.
NCERT Class 11 Biology, Chapter 9 Notes |
According to NCERT Class 11 Biology chapter 9 notes
Zwitterion structure of amino acid is defined as a structure having both charges ie..positive charge like NH4+and negative charge like COOH-.
Each amino acid at specific Ph will neither move toward cathode nor anode on applying an electric field, net charge is zero. Then, that ph is called isoelectric point.
According to ncert notes for Class 11 Biology chapter 9,
Ring isomers differ in the orientation of Oh- at hemiacetal and hemiketal carbon.
According to NCERT CLASS 11 CHAPTER 9 NOTES
F - Phenylalanine
W- Tryptophan
K - Lysine
. Y - Tyrosine
According to NCERT CLASS 11 chapter 9 notes Alpha helix structure has an intrachain H bond whereas, In a beta-pleated sheet, the H bond is between two different chains.
According to NCERT CLASS11 CHAPTER 9 NOTES
Lock and key Model by Emil.
Based on the complementarity between the shape of substrate and geometry of binding site on enzymes.
Induced fit hypothesis
According to this model, enzymes are flexible, binding happens by the conformational change in enzyme
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