In Class 12 Boards there will be Case studies and Passage Based Questions will be asked, So practice these types of questions. Study Rate is always there to help you. Free PDF Downloads of CBSE Class 12 Chemistry Chapter 14 Biomolecules Case Study and Passage-Based Questions with Answers were Prepared Based on the Latest Exam Pattern. Students can solve NCERT Class 12 Chemistry Case Study Questions Biomolecules to know their preparation level.

In CBSE Class 12 Chemistry Paper, There will be a few questions based on case studies and passage-based as well. In that, a paragraph will be given, and then the MCQ questions based on it will be asked.

Biomolecules Case Study Questions With Answers

Here, we have provided case-based/passage-based questions for Class 12 Chemistry Chapter 14 Biomolecules

Case Study/Passage-Based Questions

Case Study 1: Monosaccharides containing an aldehyde group are called aldoses while those containing a keto group are called ketoses. All monosaccharides containing five and six carbon atoms have cyclic structures, furanose (five-membered) and pyranose (six-membered). During ring formation, C₁ aldoses and C₂ in ketoses become chiral and hence all these monosaccharides exist in two forms called the α-anomer and β-anomer while C₁ and C2 are called glycosidic or anomeric carbon atoms. In contrast, stereoisomers, which differ in configuration at any other chiral carbon other than the glycosidic carbon are called epimers. Two molecules of the same or different monosaccharides combine together through glycosidic linkage to form disaccharides

Que 1. Which of the following compounds show furanose structures? 

a) Mannose
b) Galactose
c) Fructose

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Que 2. What is the relation between two molecules?
(a) Enantiomers
(b) Epimers
(c) Functional groups
(d) Anomers

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Que 3. In disaccharides, the linkage connecting monosaccharide units is called
(a) Glycogen linkage
(b) Nucleoside linkage
(c) Glycosidic linkage
(d) Peptide linkage.

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Case Study 2: Proteins are the most abundant biomolecules in the living system. The chief sources of proteins are milk, cheese, pulses, fish, meat, peanuts, etc. They are found in every part of the body and form a fundamental basis of the structure and functions of life. These are also required for the growth and maintenance of the body. The word protein is derived from the Greek word, ‘proteins’ meaning ‘primary’ or of ‘prime importance’. Chemically, proteins are polymers in which the monomeric units are the α-amino acids. Amino acids contain amino (-NH2) and carboxylic (-COOH) functional groups. Depending upon the relative position of the amino group with respect to the carboxylic group, the amino acids can be classified as α, β, and γ-amino acids. Amino acids which are synthesized by the body are called non-essential amino acids. On the other hand, those amino acids which cannot be synthesized in the human body and are supplied in the form of diet (because they are required for proper health and growth) are called essential amino acids.
Que 1. Amino acids show amphoteric behavior. Why?
a) They have an amino group
b) They have a carboxylic group
c) Both (a) and (b)
d) none of the above

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Que 2. The name of linkage joining two amino acids
a) Hydrogen bonding
b) Peptide linkage
c) Amino linkage
d) Imino joints

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Que 3. What are polypeptides?
a) 10 < α-amino acids joined together
b) amino acids joined together
c) 20 < β-amino acids joined together
d) None of the above

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Que 4. What type of bonding helps in stabilizing the α-helix structure of proteins?
a) Peptide linkage
b) Hydrogen bonding
c) Amino linkage
d) Van der waals force

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Case Study 3: When a protein in its native form, is subjected to physical changes like change in temperature or chemical changes like change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix gets uncoiled and protein loses its biological activity. This is called the denaturation of protein.
The denaturation causes change in secondary and tertiary structures but primary structures remain intact. Examples of denaturation of protein are coagulation of egg white on boiling, curdling of milk, and formation of cheese when an acid is added to milk.

(i) Mark the wrong statement about denaturation of proteins

(a) The primary structure of the protein does not change

(b) Globular proteins are converted into fibrous proteins.

(c) Fibrous proteins are converted into globular proteins.

(d) The biological activity of the protein is destroyed.

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(ii) Which structure(s) of proteins remains(s) intact during denaturation process?

(a) Both secondary and tertiary structures	(b) Primary structure only
(c) Secondary structure only	(d) Tertiary structure only

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(iii) Cheese is a

(a) globular protein	(b) conjugated protein
(c) denatured protein	(d) derived protein

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(iv) Secondary structure of protein refers to

(a) mainly denatured proteins and structure of prosthetic groups

(b) three-dimensional structure, especially the bond between amino acid residues that are distant from each other in the polypeptide chain

(c) linear sequence of amino acid residues in the polypeptide chain

(d) regular folding patterns of continuous portions of the polypeptide chain

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