FOUR-YEAR ACADEMIC PROGRAMME FOR B.Sc. (Hons) APPLIED BIOCHEMISTRY

 COURSE DESCRIPTIONS

BCH 102: INTRODUCTORY BIOCHEMISTRY (3 CREDITS)

Historical perspectives of Biochemistry. The building units of macromolecules – structures and functions of amino acids, monosaccharids, glycerol, fatty acids, choline and nitrogenous bases. Abiotic synthesis of building units. The classification and hierarchical organization of macromolecules.  Proteins – globular, fibrous, albumin, prolamin, gliadin, globulin and lignin. Lipids – phospholipids, sphingolipids, plasmologens, VLDL, HDLP, soap, micelles, membrane, e.t.c Nucleic acide – nucleosides, nucleotides, DNA, RNA. The physical and chemical properties of water, weak acids and bases, pH, pOH, pK_a, pK_b, etc. Buffer solutions. Preparation of solutions. The properties and classification of enzymes. The living cells of plants and animals – Biochemical structures, size dimension and functions of organelles.

BCH 201: INTRODUCTORY BIOMOLECULAR CHEMISTRY (2 CREDITS)

The chemical composition of living organisms. The geometry, bond strength, electronegativity, bond energies, van der waals forces, radii of carbon, nitrogen, oxygen and sulphur bondings. The three dimensional structures of simple biomolecules configuration and conformation, molecular model of small melecules, stereoisomerism and stereospecificity. Carbohydrate chemistry – classification, structure, isomerism, reactions and importance. Lipid chemistry – classifications, structures and reactions. Amino acids chemistry classification, structures and reactions.

BCH 202: INTRODUCTION TO METABOLIC PATHWAYS (2 CREDITS)

Spontaneous reaction, free energy change of reaction and activation energy. The properties, nomenclature and function of enzymes. Glycolysis, glucogenesis and pentose phosphate pathways. Tricaboxylic acid cycle and oxidative phosphorylation. Beta-oxidation and starvation (Ketone bodies). Amino acid pool, nitrogen balance, protein degradation, deamination and transamination reactions. The urea cycle. Photosynthesis: The Light and dark reactions – Calvin cycle.

BCH 212: BIOLOGICAL MACROMOLECULES   (2 CREDITS)

Carbohydrates and glycobiology – structure, activity and function. Polysaccharides – starch, glycogen, cellulose, chitin and inulin. Proteoglycans, glycosaminoglycans, peptidoglycans. Glycoprteins – lectins, selectin. Glycolipids – gangliosides, lipopolysaccharide. Analyses of carbohydrates. Protein three-dimensional structure and activity – primary structure and protein sequence determination. Secondary structures – peptide bond angle, length, rigidity and structure, Alpha-helix, Remachandran plot, Beta-conformation, Beta-turns. Tertiary structures – Fibrous proteins, alpha-Keratin, collagen, fibrin, Globular proteins-three dimensional structures, troponin, antibodies, myoglobin, ribonuclease, Iysozyme. Super-secondary structure. Quaternary structures – multimeric proteins rotational and helical symmetry. Haemoglobin, poliovirus coal protein, molecular size of proteins and limitation to size. The use of X-ray and NMR for studying protein structures, protein folding and denaturation - -chaperones and chaperonins. Nucleic acids and Nucleotides. Properties of Nucleotides, Absorption spectra, Tautomerism, phorphodiester bonds in Nucleic acids, base pairing and hydrogen bonding. Three-demensional structures of RNA – RNA, RNA, mono and polycistronic RNA. DNA-double helix, distinctive composition, A, B and Z forms hairpins and cruciforms. Non-enzymatic transformation of nucleic acids – pyrimidine dimerization, nucleic acid hybridization, denaturation of DNA .Functions of nucleotides – energy compounds, enzyme cofactors. Lipids – Glycerophospholipids, sphingolipids, gangliosides lipoproteins

BCH 222: BIOENERGETICS AND BIOCATALYSIS (2 CREDITS)

The laws of thermodynamics. Concept of free energy, entropy, high-energy compounds, free energy change for the hydrolysis of ATP, thiolesters and hig-energy compounds. Oxidation-reduction reaction, reduction potential, standard reduction potential and its measurement. Electron carries. Catalysis and activation energy – transition state reactions, Arrhenius equation, calculation of activation energy and energy of denaturation. Effect of temperature on catalysis. Kinetics of enzyme catalyzed reactions. Michealis-Mention equation, Lineweaver-Burk polt and other transformations. Effect of pH and inhibitors. Allosteric and regulatory enzymes. Purification and quantities estimation of enzymes activity. Purification tables and unites of enzyme activity.

BCH 232: PHYSIOLOGICAL CHEMISTRY (2 CREDITS)

Body fluids-Classification and composition. Blood clotting, blood groups and rhesus factor. Homeostasis regulation and disorders of acid-base balance. Homeostatic control of sugars. Renal systems- structure and functions. Nervous system-structure and function of neurons, the nerve impulse, organization of nervous system – peripheral and autonomic nervous system. Muscular system – types, structure and functions. Myocytes, actin, myosin and muscles contraction. Respiratory system – structure of the lungs, mechanism of breathing. Cardiovascular system – structure and functions. Endocrine system – the pituitary, anterior and posterior lobe hormones. Gastrointestinal tract – digestion and absorption. Liver – structure and functions.

BCH 242: COMPUTATIONAL BIOCHEMISTRY & MOLECULAR BIOLOGY (2 CREDITS)

Introduction to Internet – World wide web – Internet resources, browses, search engines, pubmed, Databases and its retrieval. Nucleotide Sequence databases and analysis, Genes and genome, - prokaryotic and eukaryotic genes. GenBank entry and Genome Database, organelle genome. Gene identification with internet recourses. Exploring human genome. Protein Sequence database – Sequence alignment and similarity search. Multiple sequence alignment. Proteonmices – analysis and internet resources. ORFs, introns, exons – Finding protein coding regions. Presdicting protein structured classifications. Phylogenetic analysis – Applications and inference. Evolution, Online and generic sources. Biochemical data analysis and management. Spread sheet applications, Microsoft excel, Microsoft Access and SPSS, other simple and multiple regression and correlation software applications.

BCH 301: PRIMARY METABOLIC PATHWAYS 1 (3 CREDITS)

Catabolism of glucose, galactose and fructose, etc., Glycolysis, regulation of glycolysis, Pasteur effect, anaerobic fermentation. Gluconeogenesis-from lactate, amino acids glycerol, Regulation of the cori cycle. The citric acid cycle and the glyoxylate cycle.Electron transport and Oxidative phosphorlation, mechanism of ATP synthesis, effect of inonphore, uncoupler and energy transfer inhibitors. Glycogenesis and glycogenolysis, regulation and synthesis of starch, sucrose and others. The pentose phosphate pathway. Lipid metabolism, dietary lipids and lipoproteins. Fatty acid oxidation, synthesis and degradation of ketone bodies. Synthesis or fatty acids, triacyglycerol, glycerophospholipids, sphingolipids, cholesterol and steroid hormones.

BCH 311: CELL AND MOLECULAR BIOLOGY 1 (3 CREDITS)

DNA structure and size chromatin and nucleoid structure, DNA supereoiling and conjugation. DNA metabolism – replication, repair and recombination. RNA metabolism – DNA transcription, reverse transcription regulation of transcription, operons, post-transcriptional processing of RNA. Protein metabolism – protein synthesis, genetic code, initiation, elongation and termination of protein synthesis, post-translation processing, protein targeting and transport, protein degradation. Mutation, mutagenic agents and cancer. Molecular description of the life cycle of Lambda, M13, HIV, etc. Organization of Prokaryotic and Eukaryotic genome, intron, exon, transposon, retrotransposen, GC, and AT content of genes, satellite DNA, palindrome, others. Melecular tools – restriction endonucleases, DNA ligases, natural and artifical vectors of gene transfer, plasmids, cosmids, virus, polymerase cheain reaction, DNA hybridization, etc.

BCH 321: INTRODUCTORY PHARMACOLOGY (2 CREDITS)

Definition of common terms in pharmacology – drugs. Source and composition. Drug development/assays. Important Pharmaceutical preparations, drug identity and nomenclature Routes of drug administration, placebo effect, drug allergy, drug idiosyncrasy. Drug interactions cummulation, synergism, tolerance, antagonism. Drug tolerance and drug resistance. General pharmacologic response to drugs – nature and mechanism. Concept of agonists, antagonists and receptors. Quantitative pharmacology – dose response, therapeutic index (TI), lethal dose, etc. Cellular metabolism in infected cells. Host parasite relationships. Biochemical basis of chemotherapy, Enzyme inhibitors as drugs. The physical basis of drug selectivity. Traditional medicine – management of malaria, sickle cell anemia, common cold, hepatitis etc. with plant extracts.

BCH 331: BIOCHEMICAL INSTRUMENTATION AND TECHNIQUES (3 CREDITS)

Microscopy, Light and electron microscopy, ion probe analysis and video microscopy.

Calomel and glass electrodes for pH measurement. Ultra filtration and dialysis. Centrifugation – principles, differential, density gradient, ultra centrifugation: analysis of subcellular fraction. Spectroscopy spectrophotometry, turbidometry, nephlometry Atomic absorption, atomic emission, spectroflourimetry. Chromatography – principles. Types – paper, thin layer, absorption, molecular exclusion, partition, affinity, ion exchange, gas-liquid, high performance, low pressure. Detection, quantification and analysis of biomolecules by chromatography. Electrophoresis cellulose acctate, agarose gel, starch gel, SDS- polyacrylamide gel isoelectric focusing detection, estimation of molecular weight of protein. Western, Northern and Southern blotting. Radioisotopic techniques – Nature of radioactivity, counting, radioactivity and data analysis, ELISA, Application in immunology and bioassays.

BCH 341: FOOD AND NUTRITIONAL BIOCHEMISTRY (2 CREDITS)

Food nutrients-carbohydrates, proteins, essential amino acids, fats, water. Food nutrients-vitamins and their co-enzyme derivatives, A, B, C, D, E, K, Lipoic acid, pantothenic acid, folic acid, biotin, cholin-structures, sources, reactions and deficiency syndrome of vitamins. Food nutrients requirement sources, reactions and deficiency syndrome of macro and micro minerals. Relationship between physiochemical and biological function of inorganic ions, ligand complexes and function. Food analysis -  proximate analysis, moisture and dry matter, organic and inorganic matter, ash. Basal Metabolic Rate (BMR), measurement and factors that influence BMR. Anutrients in food phytohaemagglutinin, protease inhibitors, phytate, phytoestrogen, sapponin, tannins, polyphenols, flatulence factors, amylase inhibitors, anti-vitamins, amino acid analogues, goitrogens, etc. Beneficial effects of anutrients. Food additives, food toxin: monosodium glutamate, artificial sweeteners, colouring, aflax. Nutritional disorders: protein energy malnutrition, obesity and diabetes. Nutritional status: recommended daily allowances. Diet and physiological stress, ageing, pregnancy and athletics.

BCH 351: BIOCHEMICAL LABORATORY TECHNIQUES (2 CREDITS)

Introduction- The work environment, health and safety, Analysis of data. Graphs bar, histogram, pi-chart and rectangle co-ordinates plot y vs x, standard curve, average, standard error, standard deviation, confidence limits, frequency, least square methods, etc. Solutions- distilled water, de-ionized water, buffer solution – titration of weak acids and bases, calculation and preparation of standard solutions. Solutions of standard ionic strength. Carbohydrate- quantitative and qualitative analysis, Molisch, Bial’s Seliwanoff, iodine, Barfoed, Benedict and Fehling tests. Estimation of starch and glycogen content – Anthrone, Phenolsulphuric acid methods. Amino Acids- qualitative and quantitative analysis; Xanthoproteic, Millions, Sakaguchi and Ninhydrin reactions etc. Lipids qualitative and quantitative analysis. Acid value of oils saponification value, isolation of fatty acids. Nucleic acids and Nucleotides – Isolation of RNA and DNA. Estimation of RNA and DNA tissue. Effect of temperature on the viscosity of DNA. Chromatography- paper, thin layer and adsorption. Separation of ink and plant pigments. Chromatography- Gel and ion exchange, separation of proteins. Electroporesis- paper and gel. Separation of haemoglobin A and S. Metabolisms: Photosynthesis isolation of chloroplast, reduction of DCPIP by chloroplast, Blood glucose levels in diabetes, Metabolic changes associated with organisms, Bioluminiscenses.

BCH 361: PLANT BIOCHEMISTRY (3 CREDITS)

Organization of plnt cells – structure of plant cell wall and function of organelles. Plant cell wall – three dimensional structure composition and function. Stages in plant development, totipotency, plant cell tissue and organ feature, seed germination and growth. Photosynthesis – C3, C4 and crasulassean acid metabolism in plants photorespiration. Nitrogen metabolism – nitrogen cycle and non-protein amino acids. Transport and storage of amino acids in plants. Classification of plant proteins. Cyanogenic glycosides – structure and toxicity. Sulphur cycle. Plant root and soil interaction. Plant exudates, symbiotic and non-symbiotic nitrogen fixation. Phytohormones and related compounds: auxins, gibberellins, cytokinins, abscisic acid, ethylene, and other plant growth regulators. Herbicides- mechanism of action, residue determination and toxicity. Nitrogen compunds-classification, structure and biosynthesis of alkaloids, chlorophyll, model and amines. Plant phenols-structure, function and biosynthesis of phenols, phenolic acids, phenylacetic acid, hydroxycinnamic acid, quinines, xanthones, stilbenes, flavonoids, lignans ans neolignans, biflavonoids, tannins and melanins. Trepenoids-structure, synthesis and function of essential oils diterpenoids, triterpenoids, steroids, carotenoids and polyisoprene. Physiochemical methods-methods of plant analysis-extraction, separation, identification and analysis of plant component, fractionation into different class of polarity.

GIT 399: SIWES (6 CREDITS)

Students Industrial Work Experience Scheme (SIWES)

BCH 401: PRIMARY METABOLIC PATHWAYS II (3 CREDITS)

Nitrogen metabolism, nitrogen cycle, nitrogen fixation, glutamine synthetase in nitrogen metabolism. Amino Acid biosynthesis and its regulation. Defects in amino acid metabolism. Synthesis of molecules derived from amino acids-prophyrins, creatine, glutathione, amino acids, others. Nucleotide and nuleic acid synthesis. Salvage and de-novo pathways and regulation. Nitrogenous excretory products – amino acid oxidation, production of urea, degradation of nucleotides, nuleic acid, purines and pyrinmidines: Lesch-Nyhan syndrome, gout. Integration and hormonal regulation of mammalian metabolism. Tissue specific metabolism, hormonal regulation of such metabolism-epinephrine, glucagons, insulin, cortisol.

BCH 402: ADVANCED ENZYMOLOGY AND REGULATORY MECHANISMS (3 CREDITS)

Kinetics of ligand binding – Boding of oxygen to heamoglobin and myglobin. Antigen-Antibody interaction. Hill’s equation, Scatched plot. Multisubstrate Kinetics – sequential, ping-pong and other mechanisms. Inhibition studies – reversible and irreversible inhibition, substrate and product inhibition – competitive, non competitive, uncompetive and mixed-type. Chemistry of enzyme catalysis, rate enhancement, binding energy, transition state stabilization, desolvation, induced fit, covalent catalysis, acid-base catalysis, proximity effect, metal ion catalysis. Effect of pH, Optimum pH and pK_a value of active site residues ionization of enzymes, enzyme-substrate complex. Effect of temperature – free energy changes, Equilibrium constant, Arrhenius equation, Vant Hoff’s equation, thermal denaturation of enzyme. Pre-study state kinetics, instrumentation and techniques. Regulatory enzymes – molecular model for allosterism, committed step enzymes, feedback and feed forward inhibitors and cumulative feedback inhibition. Regulation by covalent modification and proteolytic cleavage. Mechanism of catalysis for chymotrypsin, phosphofructokinase, ribonuclease, etc. Current literature reading.

BCH 411: FRONTIERS IN BIOCHEMISTRY, MOLECULAR BIOLOGY & BIOTECHNOLOGY (2 CREDITS)

Students are assigned topics that will expose them to current literature search and contemporary studies to be presented in weekly Departmental seminar. Presentation which must be prepared using PowerPoint and abstract of the presentation should be submitted one week before actual presentation date.

Seminar grading scheme includes, abstract, scope of content, standard of presentation, conclusion, references and response to questions.

BCH 412:BIOCHEMICAL REASONING AND SPECIAL TOPICS (2 CREDITS)

A reading list of literature is given to students at the beginning of the semester. Most of these topics may be part of the presentation in BCH 411. Practical manuals are also included. All lecturers should submit 10 - 20 objective questions with regard to topics of interest.

BCH 421: BIOLOGICAL MEMBRANE AND BIOSIGNALLING (3 CREDITS)

Structure, composition and function of biological membranes-lipids, proteins and carbohydrates. Biogenesis – isolation and characterization of membranes. Artificial membranes. Membrane dynamics phase transition, motion of membrane components, heterokaryon membrane fusion – exocytosis and endocytosis. Transport across membrane – simple and facilitated diffusion, exchange diffusion, symport, uniport, active transport – free energy of transport, primary and secondary active transport systems. Classification of ATPases, ion gradient for transport, ion-selective channels, acetylcholine receptor, porins, etc., defective ion channel, ionophores. Signal transduction features: Gated ion channels – electrical signaling, Ligand-gated ion channel, nicotinic acetylcholine receptor, Voltage-gated ion channel, neuronal action potential.  Receptor enzymes signal transductions – tryrosine-specific protein. Kinases, insulin – receptor protein kinase, G guanyl cyclase G-protein coupled receptors: beta-Adrenergic receptor – epinephrine, Camp signaling, Diacyglycerol and IP3 signaling, Calcium signaling, Sensory transduction in vision, olfaction and gestation.

BCH 422: ADVANCED CLINICAL BIOCHEMISTRY (3CREDITS)

Biochemical tests and diagnosis – basis or uses, interpretation, factors affecting tests, variations, types of specimens for tests. Specimen preservation and handling. Diagnostic enzymes – causes of release of enzymes and plasma enzymes of clinical importance. Liver disease – tests used to assess liver diseases, eg, liver function tests, bilirubin production and metabolism. Jaundice types. Metabolic disorders – diabetes mellitus, diabetes insipidus, glycogen storage disease and obesity. Disorders of lipid metabolism – lipoprotein metabolism and diseases associated with lipid metabolism. Renal diseases – clearance tests, renal failure – pre-renal, intrinsic, acute, post-renal and chronic renal failures. Nephritic syndrome and causes. Electrolyte metabolism. Gastrointestinal tract diseases – stomach function tests, pentagastrin and gastrin tests. Pancreatic function tests – direct and indirect tests. Malabsorption – causes and diagnosis. Reprodution – male and female sex hormones, puberty, menopause, amenorrhea, hirsutism, pregnancy and infertility, contraceptives. Thyroid disorders - functions, tests and disorders. Biochemistry of paediatrics and geriatrics – prenatal diagnosis.

BCH 431: BIOCHEMISTRY OF PARASITES (2 CREDITS)

Review of major tropical pathogenic viruses and bacteria, tropical parasitic protozoa and metazoan. Distribution and metabolism of inorganic substances in tropical parasites. Disturbance of host inorganic metabolism. Metabolism in parasitic infections. Distribution and metabolism of carbohydrates, proteins, lipids, nucleic acids and vitamins in tropical parasites, peculiarities of the metabolic machinery of parasites are highlighted. Respiration – aerobic and anaerobic respiration in parasites: respiratory chain oxidative phosphrylation, host-induced variations in respiration of the host. Control of parasitic infections – control of vectors, mechanism of action of insecticides, biological control of vectors, mechanism of parasitic diseases. Chemotherapy – mechanism, differences in the metabolism of carbohydrates, lipids,
 nucleic acids and proteins. Enzyme and organelle targets to be emphasized.

BCH 432: IMMUNOCHEMISTRY AND IMMUNOLOGY (3 CREDITS)

Innate and acquired immunity – features, mechanisms and determinants. Cells and organs of the immune system. Evolution of the immune system. Antigens-antigenic determinants, haptens, immunogens. Antibody structure and function – classification, polyspecific and monoclonal. Lymphocytes – isolation and function. Antigen-antibody interaction – characteristics, precipitation, lattice theory, agglutination and haemagglutination. Detection of antigen-antibody reaction – immunodiffusion immunoelectrophoriesis, fluorescence quenching, radioimmunoassay, enzyme-linked immunosorbent assay, fluorescent antibody technique. The major histocompatibility complex (MHC), MHC restriction. Cytokines. The complement system and its activation. Hypersensitivities. Immunologic tolerance, autoimmunity and immunodeficiency. Transplantation. Immunology of parasitic diseases

BCH 441: BIOTECHNOLOGY AND INDUSTRIAL BIOCHEMISTRY (2 CREDITS)

Bioreactors – principles, designs and application, Plant and animal cell culture. Fermentation technology-fermentation products – alcoholic, amino acid and secondary metabolites. Antibiotic products of biotechnology – structures, vinegar, organic flavour enhancers ogili. Strain selection and development - mutagenesis, over-production of metabolites and gene dosage. Screening and selection of micro-organism of industrial importance. Genetic Engineering for improved plants and animals, metabolic engineering, protein engineering and antibody engineering. Principles of industrial enzymology. Principle and application of cell and enzyme immobilization. Large-scale protein/enzyme purification techniques. Application of enzymes in industrial and clinical analysis. Biosenors. Industrial pollution and bioremediation. Process evaluation, development, quality control and industrial standards. Industrial experiences – invitation of industrialist for discussion of topic of interest; discussion of industrial attachment and experiences.

BCH 442: MOLECULAR BIOLOGY AND GENETIC ENGINEERING (3 CREDITS)

Mutations, site directed mutagenesis, the environment and mutagenesis, Ames test, Cancers. Recombinant DNA technology – DNA library, cDNA library, methods of engineering new products. The cell cycle and cell death – mitosis, mitotic phases, apoptosis and meiosis, regulation of cell cycle, oncogenes and tumour suppressor genes. Molecular medicine – the human genome. Structural organization, proteomics, monogenic and polygenic disorders, pre-natal diagnosis, viral infections, gene therapy.  Molecular motor proteins and functions. Structure of molecular motors and accessory proteins, formation of motile assemblies in cells. Functional properties of the biological machine. Mechanism of protein degradation. Ubiquitination and proteosome, autophagy. Proteolytic enzymes – specificities and functions. Frontiers in cell and molecular biology – current literature and discussions.

BCH 451: MICROBIAL BIOCHEMISTRY (2 CREDITS)

Classification and structure of bacterial, fungal and protozoan cells. Nutritional categorization – autotroph, heterotroph, photoautotroph, photoorganotroph, chemolithotroph and chemoogantroph. Auxotrophic organism – importance. Biosythsesis, structure and function of bacterial and fungal cell well. Metabolic pathways unique to microorganism: phosphoketolase pathway. Entner – Duodorof pathway, modification of glycolytic and pentose phosphate pathways. Antibiotics – synthesis and activities. Biochemical basis for antibacterial, antifungal and antiprotozoan action. Antiseptics and disinfections.

BCH 452: BIOCHEMICAL PHARMACOLOGY (3 CREDITS)

Drug metabolism – phases, drug metabolizing enzymes and factors affecting metabolism. Drug distribution – bioavailability, drug reservoirs: plasma protein and tissue binding, redistribution, blood-brain barrier, foetal-placental barrier. Excretion – renal, biliary and faecal excretion. Excretion by other routes – sweat, saliva, breast milk. Pharmacokinetic parameter, kinetics of drug absorption and elimination, clearance, volume distribution, half-life and route bioavailability. Neurotransmission and drugs affecting transmission. Dosage regimes – maintenance, loading and individualizing doses. Factors that determine relationship between prescribed drug dosage and drug efficacy. Pharmacogenetics.

BCH 461: ADVANCED BIOCHEMICAL METHODS (3 CREDITS)

Exposure of students to operation of avaible laboratory equipment: Practicals and assignment Preparation of dissertation/theses. Journal publication and review. Term paper presentation of mini-project in approved format. Frontiers in Biochemical instrumentation-literature reading in new techniques and instrumentation. Spectroscopic techniques – principles, instrumentation, application of x-rays, gamma-ray resonance, infra-red and Raman spectroscopy, elect spin  resonance, nuclear magnetic resonance, circular dichroism and luminometry. Mass spectrometric techniques – principles, instrumentation and applications. Mass spectrometer, electron impact ionization, chemical ionization, field ionization, ion desorption methods, ion evaporation methods, analyzers, detectors and tendem mass spectroscopy. Electrochemical techniques – principles, potentiometry and voltametry.

BCH: 499 UNDERGRADUATE RESEARCH PROJECT (2 CREDITS)

Research problems involving laboratory work in an area of interest. Instructor/ Supervisors are assigned to students. Research is to be carried out in the first and second semesters of the final year.