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Important Diagrams: Biomolecules | Biology Class 11 - NEET PDF Download

1. Zwitter Ion

A zwitter ion is a molecule or ion with both positive and negative regions of chargeIn an aqueous solution, the carboxyl group of an amino acid can lose a proton, and the amino group can accept a proton, resulting in a dipolar ion called a zwitter ion. 

B is called zwitterionic form.B is called zwitterionic form.

2.  Carbohydrates, Amino acids, Lipids

Carbohydrates: Organic compounds made up of carbon, hydrogen, and oxygen, primarily serving as a source of energy for living organisms. They can be simple sugars like glucose or complex molecules like starch and cellulose.

Amino Acids: Organic compounds with both amino and carboxyl groups attached to the same α-carbon. Their properties depend on the variable "R" group. Example: Glycine (R = H), Alanine (R = CH3).

Lipids: Hydrophobic molecules, often composed of glycerol and fatty acids. They can be fats, oils, or phospholipids. Examples include triglycerides and lecithin.

Carbohydrates, Amino acids and LipidsCarbohydrates, Amino acids and Lipids

3. Nucleic Acids

Nucleic Acids: Polymers of nucleotides forming DNA and RNA, which store and transmit genetic information. DNA contains adenine, guanine, thymine, and cytosine bases.

Important Diagrams: Biomolecules | Biology Class 11 - NEET

Nucleic Acids

4. Polysaccharides

Polysaccharides are long chains of sugars that function as energy storage or structural components in organisms. Examples include cellulose (a homopolymer of glucose), starch (energy storage in plants), and glycogen (energy storage in animals).

PolysaccharidesPolysaccharides

5. Various levels of Protein Structure

  • Primary Structure: The sequence of amino acids in a protein, determining the order from the N-terminal to the C-terminal.

  • Secondary Structure: Local folding of the protein chain into structures like α-helices and β-pleated sheets, held by hydrogen bonds.

  • Tertiary Structure: The overall 3D folding of a single protein chain, critical for its biological function.

  • Quaternary Structure: The arrangement of multiple protein subunits into a functional unit, such as in hemoglobin with its four subunits.

Various levels of Protein StructureVarious levels of Protein Structure

6. Concept of Activation Energy

The y-axis shows potential energy, and the x-axis represents the transformation of a reaction through a transition state. In exothermic reactions, the product (P) has lower energy than the substrate (S), and no extra energy is needed. Regardless of whether the reaction is exothermic or endothermic, the substrate must pass through a high-energy transition state. The energy required to reach this state is called activation energy, which enzymes lower to make the reaction easier.

Concept of activation energyConcept of activation energy

7. Effect of change in : (a) pH (b) Temperature and (c) Concentration of substrate on enzyme activity

Enzymes work best at specific temperatures and pH levels, with activity dropping outside of their optimal range. Increasing substrate concentration initially boosts reaction velocity, but it plateaus at Vmax once all enzymes are saturated. Enzyme activity can also be blocked by competitive inhibitors, which mimic the substrate and prevent binding.Effect of change in : (a) pH (b) Temperature and (c) Concentration of substrate on enzyme activityEffect of change in : (a) pH (b) Temperature and (c) Concentration of substrate on enzyme activity

Diagram Based Questions NEET

Q1: Given below are two statements:
Statement I : Amino acids have a property of ionizable nature of NH2 and COOH groups, hence have different structures at different pH. 
Statement-II : Amino acids can exist as Zwitterionic form at acidic and basic pH.
In the light of the above statements, choose the most appropriate answer from the options given below:
(a) Statement I is incorrect but Statement II is correct
(b) Both Statement I and Statement II are correct
(c) Both Statement I and Statement II are incorrect
(d) Statement I is correct but Statement II is incorrect   (NEET 2022 Phase 2)
Ans:
(d)

Important Diagrams: Biomolecules | Biology Class 11 - NEET

Option (d) is the correct answer as statement I is correct but statement II is incorrect
A particular property of amino acids is the ionizable nature of −NH2 and −COOH groups. Hence, in solutions of different pH, the structure of amino acid changes. Amino acid exists as a dipolar ion called a zwitterion at a particular pH called isoelectric point.

Q2: Which of the following describes the given graph correctly?

Important Diagrams: Biomolecules | Biology Class 11 - NEET
(a) Endothermic reaction with energy A in presence of enzyme and B in absence of enzyme.
(b) Exothermic reaction with energy A in presence of enzyme and B in absence of enzyme. 
(c) Endothermic reaction with energy A in absence of enzyme and B in presence of enzyme. 
(d) Exothermic reaction with energy A in absence of enzyme and B in presence of enzyme. 
Ans: (b) 
The graph shows the activation energies of catalyzed and uncatalyzed reations. A transition state is observed when the reactants are at the crest of the hump. At this state, they are ready to be converted to products. If the products are at a lower level than the reactants, the reaction is exothermic.

The document Important Diagrams: Biomolecules | Biology Class 11 - NEET is a part of the NEET Course Biology Class 11.
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FAQs on Important Diagrams: Biomolecules - Biology Class 11 - NEET

1. What is the structure of an amino acid and how does it relate to its function in proteins?
Ans.An amino acid consists of a central carbon atom, an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom, and a variable R group (side chain) that determines the specific characteristics of the amino acid. The structure allows amino acids to link together via peptide bonds to form proteins, which are essential for various biological functions.
2. What is a zwitterion and how does it form in amino acids?
Ans.A zwitterion is a molecule that has both positive and negative charges, resulting in a net neutral charge. In amino acids, at physiological pH, the amino group is protonated (-NH3+) while the carboxyl group is deprotonated (-COO-), leading to the formation of a zwitterionic form. This form is crucial for the solubility and reactivity of amino acids in biological systems.
3. What are nucleosides and nucleotides, and what is their significance in nucleic acids?
Ans.Nucleosides consist of a nitrogenous base attached to a sugar (ribose or deoxyribose), while nucleotides are nucleosides that also include one or more phosphate groups. Nucleotides are the building blocks of nucleic acids (DNA and RNA) and play a key role in energy transfer (ATP), signaling (cAMP), and as coenzymes.
4. What are the different types of bonds found in DNA and how do they contribute to its stability?
Ans.DNA contains several types of bonds, including phosphodiester bonds between nucleotides, hydrogen bonds between complementary nitrogenous bases (A-T and C-G), and covalent bonds within the sugar-phosphate backbone. The hydrogen bonds provide specificity in base pairing, while the phosphodiester bonds contribute to the overall stability and integrity of the DNA structure.
5. What factors affect the activity of enzymes and how can they be manipulated in a laboratory setting?
Ans.Enzyme activity can be influenced by factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators. In a laboratory setting, these factors can be manipulated by adjusting the reaction conditions, using different buffer systems, or by adding specific molecules to study their effect on enzyme kinetics and activity.
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