Acid, Base & Buffer
* Derive the Henderson-Hasselbalch equation. What are the applications of this equation?
[3.0]
* Define: (i) conjugate acid-base pair, (ii) pH indicator [2.0]
* With an example describe how can buffers maintain pH of a solution? [2.0]
* What is the pH of a buffer that is 0.12 M in lactic acid, CH₃CH(OH)COOH and 0.10 M
sodium lactate? Kₐ for lactic acid is 1.4×10⁻⁴. [2.0]
* Which solution would have the most acidic pH and why, 0.3M of HNO₃ or 0.3M of H₂SO₄?
[2.0]
* What is titration? How do you reach the end point of a titration? [2.0]
* How can you measure the pKa of an acid from the titration curve? [2.0]
* Define buffer. How does buffer work? [2.0]
* How is our blood pH maintained? [2.0]
* Explain the equation that relates pH, pKₐ and the ratio of weak acid to its conjugate base
for a buffer solution. [3.0]
* What is the pH of a buffer that is 0.12 M in lactic acid, CH₃CH(OH)COOH, and 0.10 M in
sodium lactate? Kₐ for lactic acid is 1.4×10⁻⁴. [3.0]
* Derive the Henderson-Hasselbalch equation. What are the applications of this equation?
[4.0]
* Explain how CH3 COOH/CH3 COONa, a buffer solution will resist the change in pH in that
solution of interest after addition of small H+ and OH− ion. [3.5]
* Phenolphthalein is a weak Acid Indicator (WAI). In acidic condition, this indicator remains
colourless whereas in basic condition the colour of this indicator reverts to pink. With
proper chemical justification, how could you explain the colour changing property of
phenolphthalein in acid and base considering the Ostwald’s theory? [4.0]
* Say, you have a 100 ml stock solution of 100 mg/ml ampicillin in deionized water and you
want to make 400 ml of 25 µg/ml ampicillin in nutrient agar. How much ampicillin stock and
how much nutrient agar needed to make this? Show all your works neatly. [2.5]
* Deduce "Henderson-Hesselbalch" equation. What are the applications of this equation?
[4.0]
* Define with example-hydrophobicity and hydrophilicity. [2.0]
* Deduce Henderson-Hasselbach equation. What are the applications of this equation.
[4.0]
Essential Bioelements and Biomolecules
* What are the most common bio-elements found in living beings? What properties are
common to these biogenic elements? [2.0]
* Name major classes of biomolecules that are important for all living things? Describe
their monomeric and polymeric forms with a major function. [4.0]
Carbohydrates
* What are isomers, epimers, anomers and enantiomers of glucose? How can you obtain
the optical isomer of glucose? [2.0+1.0=3.0]
* Compare the structure and properties of Mono, Di and polysaccharides. [3.0]
* What are the different substitutions found in hexose sugars. Discuss any three with an
example for each. [3.0]
* Write the structure of the three important disaccharides found in our food. [1.0]
* Mention the uses of cellulose. How do chitins differ from cellulose in structure and
function? [3.0]
* Differentiate between proteoglycans and glycoproteins with examples. [3.0]
* Write about the following heteropolysaccharides (any two): [3.0]
i. Hyaluronic acid
ii. Heparin
iii. Blood group antigens
iv. Chondroitin sulphate
* Briefly describe the properties and function of Polysaccharides. [2.0]
* Define reducing and non-reducing sugar with an example for each. Explain a test to
differentiate a reducing sugar from a nonreducing sugar? [2.0]
* Define the followings with structure and function: [3×2=6.0]
i) Starch
ii) Cellulose
iii) Chitin
* What are the three different sugar acids of aldoses? How are they formed? [2.0]
* Glucosamine, galactosamine, and mannosamine are substituents of their parent
compounds, discuss. [2.0]
* Write the chemical characteristics and biological functions of carbohydrates. [3.0]
* What is a reducing sugar? "Maltose is a reducing sugar, whereas sucrose, another
disaccharide, is not" – Explain. [4.0]
* Discuss the structural characteristics and functions of glycogen. [3.0]
* Define the following terms with appropriate examples where necessary:
i. Enantiomers
ii. Chiral carbon
iii. An aldohexose
iv. Amylose and amylopectin [1.0×4=4.0]
* Give at least two differences between glucose, galactose and fructose. [3.0]
* Aldoses can be oxidized to three different acids. Name them. [1.5]
* How are sugar alcohols formed? Write appropriate structures of three sugar alcohols.
[1.5]
* Briefly discuss the properties of Monosaccharides. 1.50]
* Define reducing sugar with an example. Explain a test to differentiate a reducing sugar
from a non-reducing sugar. 1.00]
* Write the structure of each of the following: i. A sugar containing a nitrogen, ii. A
disaccharide [1.00]
* Why do glucose, fructose and mannose give the same type of osazone? [1.50]
* Classify polysaccharides according to their structure. [2.00]
* Differentiate the structural and functional difference between Starch and Cellulose.
[1.50]
* Mention one use of each of the followings: i. Agar ii. Chitin iii. Dextran [1.50]
* Mention the important functions of a mucopolysaccharide. [2.50]
* What is hyaluronic acid? Write its function and application. [2.50]
* Briefly explain the functions of carbohydrates in biological systems. [2.0]
* What is reducing sugar? “Maltose is a reducing sugar, whereas sucrose, another
disaccharide, is not” ---Explain. [3.5]
* Briefly describe the procedure of estimating reducing sugar in a supplied sample. [4.5]
* Classify carbohydrates. What are the reducing sugars? Write down a chemical test with
the explanation for detecting the reducing sugars. [5.0]
* Explain the optical properties of glucose. Why can we store glycogen but not glucose in
our body? Explain with reasons. [5.0]
* What are lectin, selectin, and integrin? With appropriate example, describe the
quantification of sugar. [2.5]
* Define with a representative structure of the following- Glycolipid, Sphingomyelin,
Phosphatidyl ethanolamine and Cardiolipin (diphosphatidyl glycerol). [6.0]
* Write the chemical characteristics and biological functions of carbohydrates. [4.0]
* Briefly describe the identifying test of carbohydrate. [3.0]
* Discuss the structural characteristics and functions of glycogen. [3.0]
Nucleic Acids
* Compare and contrast between nucleotides and nucleosides. [3.0]
* Explain the central dogma of molecular biology. [2.0]
* Schematically explain the Watson and Crick model of DNA. [3.0]
* DNA provides a template for replication and transcription - briefly discuss. [2.0]
* Describe the salient features of nucleic acids that makes them a biologically important
biopolymer. [2.0]
* With appropriate diagram, mention the structural and functional differences between
DNA and RNA. [3.0]
* Name two important nucleotides that are not part of DNA or RNA and mention the roles
they play in cells. [2.0]
* 'DNA provides a template for replication and transcription'- briefly discuss. [3.0]
* Write short notes on any four of the followings: [4×2.5=10.0]
a) Watson and Crick DNA structure
b) Experimental proof that DNA is the genetic material
c) Buffer
d) Proteoglycans and glycoproteins
e) Ion product of water
* Differentiate between:
i. Nucleoside and Nucleotide, ii. Purine and Pyrimidine. [2.0×2=4.0]
* How are nucleotides linked in nucleic acids? [1.0]
* Draw and label the Watson and Crick model of DNA. [2.5]
* Name the three major RNAs. Differentiate DNA from RNA. [2.5]
* Draw the structure of a nucleotide and a nucleoside. [1.00]
* Why are nucleic acids essential biopolymers? [1.50]
* Differentiate between the structure and function of DNA and RNA. [2.50]
* Explain the composition of Nucleic Acids. Describe the types of nucleic acids available.
[4.0]
* “Only purine-pyrimidine pairs fit inside the double helix” – considering the base pairing of
DNA double helix justify the statement. [3.0]
* The base composition of a virus was found to be 11% A, 32 % G, 18 % U and 39 % C. Is
this a DNA or a RNA virus? Is it single-stranded or double-stranded molecule? Justify your
predictions. [3.0]
* Which two types of chemical interaction stabilize the double helix? [2.0]
* Describe the Base Ratio Experiment executed by Erwin Chargaff focusing on the method
& interpretation. [3.0]
* Compare and contrast among NTPs, dNTPs and ddNTPs. [2.5]
* The base composition of a virus was found to be 11% A, 32% G, 18% U and 39% C. Is this
a DNA or RNA virus? How can you tell? Is it single-stranded or double-stranded? How can
you tell? [1.0+1.5=2.5]
* Why is RNA less stable than DNA? Describe the reasoning behind this. [1.5]
* How is noncoding RNA different from coding RNA? Articulate the essential roles of several
diverse types of noncoding RNA within the cell. [1.0+3.0=4.0]
* What is transcriptome of a cell? Do you think noncoding RNA is component of
transcriptome? Justify your stand. [1.5]
* Why do mRNA molecules have short half-lives compared to other RNA molecules? Give
the proper scientific reasoning behind this. [2.0]
* Check whether the given sequence ‘TGCGATACTCATCGCA’ will form any hairpin-like
structure or not. If yes, draw the structure predicted. [1.0]
* Considering the animal cell, name the organelle that contains its own genetic material? Is
there any biological role of this genetic material? Describe briefly. [2.0]
* Describe the structure of nitrogenous basis present in nucleic acids. Add a note on
tautomerism. [3.0]
* The backbone of nucleic acid structure is 3'-5' phosphodiester bridge' – Justify. [3.0]
* Discuss the salient features of Watson - Crick model of DNA. [4.0]
Amino Acids, Peptides & Proteins
* Write down the chemical properties of amino acids. [5.0]
* What is simple protein? Classify simple proteins into various groups. [2.5]
* Show the structures of amino acids with:
(i) an aromatic ring
(ii) an imidazole group
(iii) an indole group
(iv) a sulphur containing side chain. [4.0]
* Show how a peptide bond is formed. [2.0]
* What do you understand by protein's:
(i) primary
(ii) secondary
(iii) tertiary
(iv) quaternary structures? [4.0]
* Briefly mention the metabolic functions carried out by different proteins. [2.5]
* What is Zwitter ion? Describe the acid-base properties of amino acids at different pH.
[2.5]
* Write down the chemical properties of amino acids. [5.0]
* Define peptide and mention the salient features of peptide bond and classify peptides.
[2.5]
* What is simple protein? Classify simple proteins into various groups citing example. [2.5]
* Why are amino acids zwitter ions? [1.0]
* Explain the reactions of amino acids with Ninhydrin reagents. [3.0]
* How can you identify Arginine? [2.0]
* What is Zwitter ion? Describe the acid-base properties of amino acids at different pH.
[2.5]
* Write down the chemical properties of amino acids. [5.0]
* Define peptide and mention the salient features of peptide bond and classify peptides.
[2.5]
* What is simple protein? Classify simple proteins into various groups citing examples.
[2.5]
* What is Zwitter ion? Describe the acid-base properties of amino acids at different pH.
[2.5]
* Classify amino acids on the basis of their nutritional value and metabolites. [2.0]
* Define peptide and mention the salient features of peptide bond and classify peptides.
[3.0]
* What is a simple protein? Classify simple proteins into various groups with examples.
[2.5]
* Amino acids can be classified into four groups based on their polarity. Cite examples of
two amino acids with structure from each group. [3.0]
* Write notes on the following: [2.0]
i. Zwitterion and Isoelectric point
ii. α-helix and β-pleated sheet
* What are the active structure of proteins? Discuss the interactions involved in such
structures. [2.0]
* Classify proteins based on their functions with examples. [3.0]
Enzymes
* What are apoenzymes and holoenzymes? Mention the salient features of active site of an
enzyme. [3.0]
* Explain the association of substrate concentration with reaction rate. [2.5]
* What is the significance of Km and Vmax? [2.0]
Km is a measure of the enzyme's affinity for its substrate. This
Vmax (Maximum reaction velocity): This is the
value represents the substrate concentration at which the
highest speed at which an enzyme can catalyze a
reaction velocity reaches half of its maximum (Vmax). A lower
reaction when fully saturated with substrate. It
Km value indicates a higher affinity, meaning the enzyme can
reflects the overall catalytic efficiency of the enzyme
reach half-maximal velocity at a lower substrate concentration.
under optimal conditions. Indicates the effect of
Conversely, a higher Km indicates a lower affinity, requiring
increasing enzyme concentration with reaction rate.
more substrate to reach half-maximal velocity.
* How does amylase differ from amylopectin? [1.0]
* Depict the effect of substrate concentration on reactions with/without enzyme catalysis.
[2.5]
* Explain the Michaelis-Menten Equation for enzyme catalyzed reactions and derive the
steady state of Michaelis-Menten Equation. [4.0]
* What is apoenzyme and holoenzyme? Mention the salient features of active site of an
enzyme. [2.5]
* Why some enzymes are used in clinical diagnosis? List some enzymes used for clinical
diagnosis. [2.0]
* Citing examples classify enzymes into various functional groups. [3.0]
* What is apoenzyme and holoenzyme? Mention the salient features of active site of an
enzyme. [2.5]
* Why some enzymes are used in clinical diagnosis? List some enzymes used for clinical
diagnosis. [2.0]
* Citing examples, classify enzymes into various functional groups. [3.0]
* Discuss the effect of the following factors on enzymatic reaction:
(i). Substrate concentration (ii) Temperature and (iii) pH [2.0]
* Explain the following terms with example:
(i) Cofactor (ii) Coenzyme and (iii) Prosthetic group. [3.0]
* Depict the effect of substrate concentration on reactions with/without enzyme catalysis.
[2.5]
* Explain the Michaelis-Menten Equation for enzyme catalyzed reactions and derive the
steady state of Michaelis-Menten Equation. [4.0]
* What is apoenzyme and holoenzyme? Mention the salient features of active site of an
enzyme. [2.5]
* Why some enzymes are used in clinical diagnosis? List some enzymes used for clinical
diagnosis. [2.0]
* Explain the following terms with example: [3.0]
(i) cofactor (ii) coenzyme (iii) prosthetic group
* Describe the significance of enzymes in different chemical reactions. [2.0]
* “Different factors affect the enzyme reaction velocity” — explain this statement. [3.5]
* How is enzyme activity regulated in biological system? [2.0]
* How does substrate concentration effects velocity of enzymatic and non-enzymatic
reactions? [2.5]
* Briefly describe the cholesterol quantification method by enzyme. [1.5]
* Explain Michaelis-Menten equation for enzyme catalyzed reaction and derive the steady
state of Michaelis-Menten equation. [3.5]
* Depict the effect of substrate concentration on reactions with/without enzyme catalysis.
[2.5]
* Explain the Michaelis-Menten equation for enzyme catalyzed reactions and derive the
steady state of Michaelis-Menten equation. [4.0]
* What is apoenzyme and holoenzyme? Mention the salient features of active site of an
enzyme. [2.5]
* Why some enzymes are used in clinical diagnosis? List some enzymes used for clinical
diagnosis. [2.0]
* Citing examples, classify enzymes into various functional groups. [3.0]
* What are apoenzyme and holoenzyme? How can you differentiate between co-factor, co-
enzyme and prosthetic group? [2.0]
* Classify enzymes on the basis of reactions they catalyze. Give example of each class.
[3.0]
* Cite factors affecting enzyme activity. What do you understand by Km and Vmax of an
enzyme catalyzed reaction? [ 3.0]
* Mention the salient features of active site.
Lipids
* Write down the functions and clinical significance of lipids. [2.5]
* What are triglycerides? Briefly describe the hydrolysis, saponification, hydrogenation and
oxidation reactions of triglycerols. [4.0]
* Define acid value, saponification value and iodine number of fats. Briefly describe the
cholesterol quantification procedure. [3.5]
* Write down the functions and clinical significance of lipids. [2.0]
* What is triglyceride? Briefly describe the hydrolysis, saponification, hydrogenation and
oxidation reactions of triglycerols. [3.0]
* Define acid value, saponification value and iodine number of fats. Briefly describe the
cholesterol quantification procedure. [3.0]
* Write down the functions and clinical significance of lipids. [2.0]
* What is triglyceride? Briefly describe the hydrolysis, saponification, hydrogenation and
oxidation reactions of triglycerols. [3.0]
* Define acid value, saponification value and iodine number of fats. Briefly describe the
cholesterol quantification procedure. [3.0]
* Write down the hydrolysis and saponification reactions of triacylglycerol. [2.5]
* How can you determine cholesterol concentration? [2.5]
* Write down the functions and clinical significance of lipids. [2.0]
* What is triglyceride? Briefly describe the hydrolysis, saponification, hydrogenation and
oxidation reactions of triglycerols. [3.0]
* Define acid value, saponification value and iodine number of fats. Briefly describe the
cholesterol quantification procedure. [3.0]
* Depict the significance of lipids. [2.0]
* Discuss the physiological effects of trans fatty acids. [2.5]
* Describe the chemical reactions of triacylglycerols. [4.0]
* Write down the functions and clinical significance of lipids. [2.0]
* What is triglyceride? Briefly describe the hydrolysis, saponification, hydrogenation, and
oxidation reactions of triglycerols. [3.0]
* Define acid value, saponification value and iodine number of fats. Briefly describe the
cholesterol quantification procedure. [3.0]
Vitamins
* Write down structure of Vitamin A and its role in vision. [2.0]
* Write down the chemical properties and functions of different B Vitamins. [3.0]
* Write down the chemical properties and functions of different B Vitamins. [3.0]
* Write down structure of Vitamin A and its role in vision. [2.0]
* Write down the structure of Vitamin A and its role in vision. [2.0]
* Mention the biochemical role, deficiency symptoms and chief sources of the following
vitamins:
i. Folic acid
ii. Thiamine
iii. Vitamin B₁₂
iv. Riboflavin [2.0×4=8.0]
* Show the structure of the coenzymic forms of the following vitamins:
i. Niacin
ii. Pantothenic acid [1.0×2=2.0]
* Write down structure of Vitamin A and its role in vision. [2.0]
* Write down the metabolic functions regulated by different vitamins. [1.5]
* Write down the structures and functions of different B vitamins. [4.5]
* Briefly describe the structure and chemical functions of vitamin D and vitamin K. [4.0]
* Write down the structure of Vitamin K1 and K2. Show the significance of Vitamin K in
hematology. [2.0]
* Define vitamins. Name fat soluble and energy-releasing vitamins. [3.0]
Bioenergetics
* What is oxidative phosphorylation? Briefly describe the chemiosmotic theory. [2.5]
* What are the purposes of high energy molecules in metabolism? Cite some of such
molecules and their role. [2.5]
* Define entropy and entropy change. [1.0]
* What is standard state of a material? Briefly define and correlate spontaneous, reversible
and irreversible processes. [2.5]
* Define “free energy” and “steady state”. [1.5]
* Explain spontaneous, reversible and irreversible process. [2.0]
* What is the first law of thermodynamics? Explain this law in different thermal processes.
[3.0]
* Define entropy and entropy change. [1.0]
* What is standard state of a material? Briefly define and correlate spontaneous, reversible
and irreversible processes. [2.5]
