CSIR NET Life Sciences Molecules And Their Interaction Relevant To Biology Syllabus

Molecules And Their Interaction Relevant To Biology syllabus — full chapter and topic list

Expand any chapter to see its topics and sub-topics. This is the whole examinable outline for Molecules And Their Interaction Relevant To Biology in CSIR NET Life Sciences, not a summary of it.

1. 1

   Structure of Atoms, Molecules and Chemical Bonds

   2 topics

   • Structure of Atoms
   • Chemical Bonds
2. 2

   Composition, Structure and Function of Biomolecules

   5 topics

   • Carbohydrates
   • Lipids
   • Proteins
   • Nucleic Acids
   • Vitamins
3. 3

   Stabilizing Interactions

   4 topics

   • Van der Waals
   • Electrostatic
   • Hydrogen Bonding
   • Hydrophobic Interaction
4. 4

   Principles of Biophysical Chemistry

   5 topics

   • pH
   • Buffer
   • Reaction Kinetics
   • Thermodynamics
   • Colligative Properties
5. 5

   Bioenergetics

   5 topics

   • Glycolysis
   • Oxidative Phosphorylation
   • Coupled Reaction
   • Group Transfer
   • Biological Energy Transducers
6. 6

   Principles of Catalysis

   4 topics

   • Enzymes and Enzyme Kinetics
   • Enzyme Regulation
   • Mechanism of Enzyme Catalysis
   • Isozymes
7. 7

   Conformation of Proteins

   4 topics

   • Ramachandran Plot
   • Secondary Structure
   • Domains
   • Motif and Folds
8. 8

   Conformation of Nucleic Acids

   3 topics

   • Helix (A, B, Z)
   • t-RNA
   • Micro-RNA
9. 9

   Stability of Proteins and Nucleic Acids

   overview

   Examined as a single unit within Molecules And Their Interaction Relevant To Biology — no further topic split in the official outline.

10. 10

    Metabolism of Biomolecules

    5 topics

    • Carbohydrates
    • Lipids
    • Amino Acids
    • Nucleotides
    • Vitamins

Molecules And Their Interaction Relevant To Biology flashcards for CSIR NET Life Sciences

22 of 51 cards from the Molecules And Their Interaction Relevant To Biology deck — real questions with worked answers.

1. What are the four main shells (energy levels) of an atom labeled, and how many electrons can the first two hold?

   Shells are labeled K, L, M, N. The K shell holds a maximum of 2 electrons; the L shell holds a maximum of 8 electrons (2n^2 rule).

2. Distinguish a covalent bond from an ionic bond.

   A covalent bond forms by sharing electron pairs between atoms; an ionic bond forms by complete transfer of electrons from one atom to another, producing oppositely charged ions held by electrostatic attraction.

3. Rank the four weak (non-covalent) interactions important in biology by typical bond energy, from weakest to strongest.

   Van der Waals (weakest, ~1 kJ/mol) < hydrogen bonds (~2-30 kJ/mol) ≈ hydrophobic interactions < electrostatic/ionic interactions (strongest of the non-covalent, ~20 kJ/mol in vacuum, weaker in water).

4. What is a hydrogen bond and what is its typical bond length and energy?

   A hydrogen bond is an attraction between a hydrogen covalently bonded to an electronegative donor (N, O, F) and an electronegative acceptor atom. Typical length ~0.27-0.31 nm; energy ~2-30 kJ/mol.

5. What drives the hydrophobic interaction in aqueous solution?

   It is entropy-driven: nonpolar groups cluster together to minimize disruption of the hydrogen-bonded water network, releasing ordered water and increasing the overall entropy of the system.

6. What are Van der Waals forces and what is the Van der Waals (contact) distance?

   Weak, transient attractions from induced dipoles (London dispersion) between nearby atoms. They become attractive as atoms approach, reach optimum at the Van der Waals contact distance (sum of Van der Waals radii), then turn strongly repulsive at closer range.

7. State the general empirical formula of carbohydrates and give the three major classes by size.

   General formula (CH2O)n. Classes: monosaccharides (single sugars, e.g., glucose), oligosaccharides (a few sugars, e.g., sucrose), and polysaccharides (many sugars, e.g., starch, glycogen, cellulose).

8. Differentiate aldose from ketose sugars and give an example of each.

   An aldose has its carbonyl group as a terminal aldehyde (e.g., glucose); a ketose has its carbonyl as an internal ketone (e.g., fructose).

9. What glycosidic linkages distinguish starch, glycogen, and cellulose?

   Starch (amylose) is alpha-1,4 with alpha-1,6 branches (amylopectin); glycogen is alpha-1,4 with frequent alpha-1,6 branches; cellulose is beta-1,4 linked glucose, giving a rigid, indigestible fiber.

10. Classify lipids into their major types.

    Major lipid types: fatty acids, triacylglycerols (fats/oils), phospholipids, glycolipids, sphingolipids, steroids (e.g., cholesterol), and waxes.

11. What structural difference distinguishes a saturated from an unsaturated fatty acid?

    A saturated fatty acid has no carbon-carbon double bonds (straight chain, packs tightly, solid); an unsaturated fatty acid has one or more C=C double bonds (usually cis, introducing kinks, lower melting point, liquid).

12. Describe the amphipathic nature of a phospholipid.

    A phospholipid has a hydrophilic (polar) phosphate-containing head group and two hydrophobic fatty acid tails, allowing it to form bilayers and micelles in water.

13. How many standard amino acids exist and what is their general structure?

    There are 20 standard amino acids. Each has a central alpha-carbon bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen, and a variable R side chain.

14. Name the amino acid that breaks alpha-helices and explain why.

    Proline. Its side chain forms a rigid ring locking the backbone, and it lacks the amide N-H needed for the helical hydrogen bond, so it acts as a helix breaker (also glycine, which is too flexible).

15. What is the isoelectric point (pI) of an amino acid?

    The pH at which the amino acid carries no net electrical charge (zwitterion form); for a simple amino acid pI = average of the two relevant pKa values.

16. What are the components of a nucleotide?

    A nucleotide consists of a nitrogenous base, a pentose sugar (ribose or deoxyribose), and one or more phosphate groups. (A nucleoside lacks the phosphate.)

17. Distinguish purines from pyrimidines and list members of each.

    Purines are double-ring bases: adenine (A) and guanine (G). Pyrimidines are single-ring bases: cytosine (C), thymine (T, in DNA), and uracil (U, in RNA).

18. State Chargaff's base-pairing rules for double-stranded DNA.

    A pairs with T (2 hydrogen bonds) and G pairs with C (3 hydrogen bonds); therefore %A = %T and %G = %C, and purines = pyrimidines.

19. Classify vitamins by solubility and give examples.

    Fat-soluble vitamins: A, D, E, K (stored in body). Water-soluble vitamins: B-complex (B1, B2, B3, B5, B6, B7, B9, B12) and vitamin C (not stored, excreted).

20. Which vitamins serve as precursors of the coenzymes NAD+/NADP+, FAD, and coenzyme A?

    Niacin (B3) -> NAD+/NADP+; Riboflavin (B2) -> FAD/FMN; Pantothenic acid (B5) -> coenzyme A; Thiamine (B1) -> TPP.

21. Give the Henderson-Hasselbalch equation.

    pH = pKa + log([A-]/[HA]), where [A-] is the conjugate base concentration and [HA] is the weak acid concentration.

22. What is a buffer and when is its buffering capacity maximal?

    A buffer is a solution of a weak acid and its conjugate base that resists pH change on adding acid or base. Capacity is maximal when pH = pKa (equal concentrations of acid and conjugate base).

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