Tamil Nadu HSE First Year Biochemistry study plan

Define biochemistry and distinguish it from allied disciplines, listing the four major classes of biomolecules and the bonds that assemble each

Draw and label the functional groups (hydroxyl, aldehyde, keto, carboxyl, amino, phosphate, sulfhydryl) and classify given structures as biomolecules

Explain the properties of water, hydrogen bonding, pH, buffers and the Henderson–Hasselbalch relationship, and calculate the pH of a buffer from given pKa and ratio values

Classify carbohydrates as monosaccharides, disaccharides and polysaccharides and assign D/L and reducing/non-reducing status to named examples

Describe the structure of glucose (open chain and pyranose ring) and the glycosidic linkages in sucrose, lactose, maltose and glycogen

Outline glycolysis step by step, naming enzymes, ATP/NADH yield and the regulatory steps (hexokinase, phosphofructokinase-1, pyruvate kinase)

Compare glycogenesis, glycogenolysis, gluconeogenesis and the pentose phosphate pathway in terms of purpose, tissue site and key enzymes

Describe the biological importance of mucopolysaccharides and glycoproteins with one named example each

Classify the 20 standard amino acids by side-chain nature (nonpolar, polar, acidic, basic, aromatic) and identify the nutritionally essential ones

Explain the zwitterion concept, isoelectric point and the titration curve of a simple amino acid such as glycine

Distinguish primary, secondary, tertiary and quaternary protein structure and name the bonds stabilizing each level

Describe the alpha-helix and beta-pleated sheet, and explain denaturation with two named denaturing agents and their effect on function

Classify lipoproteins (chylomicrons, VLDL, LDL, HDL) by density, composition and transport role, and relate them to clinical risk

Describe the structure of triglycerides, phospholipids, cholesterol and free fatty acids, and explain the amphipathic nature of membrane lipids

Explain beta-oxidation of a saturated fatty acid: activation, carnitine shuttle, four repeating reactions, and ATP yield for palmitate

Define enzyme, apoenzyme, cofactor, coenzyme, holoenzyme and isoenzyme with one example of each

Explain the lock-and-key and induced-fit models and describe how enzymes lower activation energy

Derive and interpret Michaelis–Menten kinetics, define Km and Vmax, and compare competitive, non-competitive and uncompetitive inhibition on a Lineweaver–Burk plot

List factors affecting enzyme activity (pH, temperature, substrate and inhibitor concentration) and describe two named clinical enzyme assays

Describe the structure of DNA and RNA, base pairing, Chargaff's rules and the central dogma, and outline semi-conservative replication

Classify vitamins as fat-soluble and water-soluble, and state the biochemical function, deficiency disease and one rich food source for each

Match water-soluble vitamins to their coenzyme forms (thiamine to TPP, riboflavin to FMN/FAD, niacin to NAD/NADP, pyridoxine to pyridoxal phosphate) and explain their role in metabolism

List the major macro- and micro-minerals with one physiological function and one deficiency disorder each

Explain bioenergetics terms: free energy, exergonic and endergonic reactions, high-energy compounds and the role of ATP as energy currency

Outline the electron transport chain, oxidative phosphorylation and chemiosmotic coupling, and state the ATP yield from NADH and FADH2

Describe the TCA cycle in sequence, naming all eight steps, enzymes and the coenzymes reduced at each step

Explain the urea cycle, transamination and deamination, and relate ammonia detoxification to the TCA cycle

Trace the fate of the carbon skeleton of amino acids into glucogenic and ketogenic pathways

Summarize lipid and carbohydrate metabolic interconversion and identify the key regulatory enzymes of each pathway

Calculate the total ATP yield from complete oxidation of one glucose molecule, accounting for glycolysis, pyruvate dehydrogenase, TCA and shuttle costs

Describe the principles of spectrophotometry, colorimetry and chromatography, and explain how a standard curve is used for quantification

Explain the clinical significance of blood glucose, urea, creatinine, cholesterol and liver enzyme measurements, and state normal reference ranges

Outline the principles of PCR, gel electrophoresis and DNA sequencing at an introductory level

Explain mutations, DNA repair and the basics of recombinant DNA technology with one application each

Interpret a simple set of given laboratory values and state the likely biochemical abnormality in each case

Revise all nine domains using a spaced schedule, allocating more time to the four highest-weight domains

Solve at least three full-length timed practice papers under exam conditions and mark them against the answer key

Re-derive from memory the glycolysis, TCA and urea cycle pathways and the Michaelis–Menten and Lineweaver–Burk relationships

Compile and re-read a personal error log, converting each recurring mistake into a corrected one-line rule

Rehearse definitions, normal values and deficiency diseases as rapid recall drills