Proposed/Revised

BIOCHEM-301           ELEMENTARY BIOCHEMISTRY                           3(2 -1)

Course Learning Outcomes

By the end of this course students will be able to;

1. Students will be able to understand the knowledge of buffers and will also be able to learn its preparation practically.

2. Students will learn the basic knowledge about enzymes.

3. Students will be able to understand basics of major biomolecules like carbohydrates, lipids, Proteins and Nucleic acids.

4. Students will practically learn the qualitative/quantitative analysis of biological molecules that are also nutritional important like carbohydrates, proteins, lipids etc.

Theory  

A general introduction to the science of biochemistry and its importance. Ionization of water, weak acid and weak bases, Define and describe pH, buffers, diffusion, osmosis and osmotic pressure. Enzymes: Classification, nomenclature, characteristics, coenzymes, cofactors and prosthetic groups. Mechanism of enzyme action. Enzyme inhibition. Carbohydrates: Classification, characteristics, aerobic and anaerobic oxidation of glucose; glycolysis, citric acid cycle, Electron transport chain (ETC) and fermentations, biological functions of carbohydrates. Lipids: Composition and classification, structure of saturated and unsaturated fatty acids and their properties, characteristics of fats and oils, general metabolism of fats and oils. Proteins: Composition and classification, characteristics and classification of amino acids, peptides and level of structural organization of proteins, physiological function and general metabolism of proteins. Nucleic acids: Chemical composition, structure of DNA and RNA and its types. A general overview of central dogma of molecular biology.

Practical

pH metry and determination of pH value of biological fluids. Preparation of buffers of definite pH. Estimation of optical activity by polarimetry. Qualitative analysis of carbohydrates. Qualitative analysis of urine for normal and abnormal constituents like albumins, acetone bodies and sugar. Estimation of glucose in biological fluids. Determination of acid, saponification and iodine values of fats/oils. Estimation of lactose and casein in milk.

Suggested Readings

1.       Ahmad, M. 2019. Essentials of Medical Biochemistry Vol-I. 9th Ed. Nishtar Publications Press. 10A Model town Multan.

2.       Boyer, R. F. 2012. Biochemistry Laboratory, Modern theory and techniques. 3^rd Ed. Pearson Education, New Jersey, USA

3.       Murray, R. K., D. A. Bender, K.M. Botham, P. J. Kennelly, V. W. Rodwell and P. A. Weil. 2021. Harper’s Illustrated Biochemistry. 32^nd  Ed. MvGraw Hill, NY, USA

4.       Nelson, D. L. and M. M. Cox. 2021. Lehninger Principles of Biochemistry. 8^th Ed. WH Freeman & Company, NY, USA

5.       Nigam, A and A. Archana . 2008. Lab  manual in Biochemistry, Immunology and Biotechnology. 3^rd Ed Tata Mcgraw Hill Publishing Company (Pvt.) Ltd. New Dehli, India

6.       Sawhney, C. K. and R. Singh. 2014. Introductory Practical Biochemistry. 5^th Edition. Norosa Pub. House, New Dehli, India

BIOCHEM-302                       BASIC BIOCHEMISTRY                  3(3-0)

Course Learning Outcomes

By the end of this course students will be able to;

The students will learn about basic biochemistry. The objectives of this course include, learning about biomolecules such as Carbohydrates, Proteins, lipids and nucleic acids. It will include basic as well as advance topics about these biomolecules

Theory

Introduction to Biochemistry, pH & its importance, Buffer, Henderson-Hasselbalch equation, Carbohydrates: Introduction to carbohydrates, Classification of carbohydrates, Glycosidic linkages & Glycosides, Isomers, Optical activity & rotations, Chemical properties of monosaccharides, structure and functions of important monosaccharide, Homopolysaccharide, Heteropolysaccharides.

Proteins: Introduction to Proteins, Classification of proteins, Structure and Classification of amino acids, Amphoteric properties of amino acids, concept of Isoelectric pH Peptide Linkage, Primary, Secondary, Tertiary and Quaternary structure of proteins.

Enzymes: General Characteristics and classification of enzyme, Enzyme Activity and factors effecting enzyme activity, Enzyme Kinetics.

Lipids: Introduction to Lipids, structure &  classification of fatty acids, nomenclature of fatty acids, Physical properties of fatty acids and triglycerides, Chemical Properties of fatty acids and triglycerides, Sterols and cholesterol, Prostaglandin and their physical role.

Nucleic Acids: General Introduction to nucleic acids, Structure and Functions of DNA and RNAs, Central Dogma in molecular biology, Structural and molecular organization of genomes in prokaryotes and eukaryotes.

Suggested Readings:

1.                                                                      Nelson, D.L. and M.M. Cox. 2017. Principles of Biochemistry, 7^th Edition, Worth Publishers.

2.                                                                      Boyer, R.F. 2014. Modern Experimental Biochemistry. 3^rd Edition. The Benjamin / Cummings Publishing Co., USA

3.                                                                      Stryer, L. 2012. Biochemistry, 7^th Edition, W. H. Freeman and Co. Lab Manual in Biochemistry, Immunology and Biotechnology, Arti Nigram, Archana Ayyagari. Tata McGraw-Hill Publishing Company Limited, New Delhi.

4.                                                                      Murray, R., D. Bender, K.M. Botham, P.J. Kennelly, V. Rodwell and P.A. Weil. 2015. Harper’s Illustrated Biochemistry, 30^th edition. The McGraw-Hill companies Inc. USA. ISBN-10: 0071825347

5.                                                                      Voet, D. and J.G. Voet. 2010. Biochemistry 4^th Edition John Wiley & Sons. USA. ISBN-10: 0470917458

6.                   Karp, G. 2015. Cell and molecular Biology, 8^th edition, Wiley Publishers. ISBN-10: 1118886143.

PROPOSED/REVISED

BIOCHEM-303                BIOCHEMISTRY OF METABOLISM                   3(3-0)

Course Learning Outcomes

By the end of this course students will be able to;

1.      Learn anabolic and catabolic pathways of carbohydrate, lipid, protein and nucleic acids

2.      Understand the principles of intermediary metabolism

3.      Explain the major mechanisms of metabolic control and cellular energy transduction processes

Contents

Introduction of metabolism; Carbohydrate metabolism: Glycolysis and Krebs cycle, their regulation and energy production, Pentose phosphate shunt, Glucoronic acid pathway, Glucogenesis, glycogenesis, glycogenolysis, gluconeogenesis, Metabolism of fructose, galactose and lactose; Introduction to protein and amino acids metabolism: Synthesis and degradation of non-essential amino acids, Fate of ammonia and keto-acids, Urea cycle and its importance, glutathione and creatinine formation, Catabolism of non-essential amino acids; Introduction to lipid metabolism: Beta-oxidation of even number and odd number fatty acids, Omega and Alpha oxidation of fatty acids, Beta-oxidation of fatty acids, Oxidation of respiratory chain, Biosynthesis of fatty acids, triglycerides, prostaglandins and cholesterol, Factors affecting cholesterol level in plasma, Transportation of lipids, Role of adipose tissue in fat metabolism, Ketogenesis and use of ketone bodies, metabolism of bile salts and bile acids; Basics of nucleic acid metabolism; Intermediary metabolism of carbohydrates, fats and proteins; Oxidative phosphorylation and bioenergetics.

Suggested Reading

1.       Ahmad, M. 2011. Essentials of Medical Biochemistry. Vol. I.  8^th ed. Merit Publishers, Lahore, Pakistan.

2.       Emine E. Abali, Susan D. Cline, David S. Franklin, Susan M. Viselli. Ferrier, D. R. 2021. Biochemistry: Lippincott’s Illustrated Reviews. 8^th ed.  Wolters. Kluwer Publishing Company, Netherland.

3.       Nelson, D.L and M.M. Cox. 2021. Lehninger Principles of Biochemistry. 8^th ed. WH Freeman and Company, New York, NY, USA. 

4.       Victor Rodwell, David Bender, Kathleen Botham, Peter Kennelly, P. Anthony Weil. 2018. Harper’s Illustrated Biochemistry. 31^st ed McGraw-Hill Education / Medical. New York, NY, USA.

BIOCHEM-304            PHARMACEUTICAL CHEMISTRY IIA                     4(3-1)

                                       (BIOCHEMISTRY)   

Course Learning Outcomes

By the end of this course students will be able to;

To make the students understand the chemical composition, classification, characteristics  and pharmaceutical importance of  carbohydrates,  lipids, proteins and amino acids, nucleic acids, vitamins, hormones and enzymes and importance of pharmaceutical biochemistry in health profession.

Theory

General Introduction and Basic Biochemical Principles: Role of Pharmaceutical Biochemistry in the health profession. Nature of biochemical reactions.

Basic Chemistry of Biomolecules: (Nature, Classification etc.) Carbohydrates: Chemistry, Classification, Reactions of Carbohydrates, Optical activity, Biological and pharmaceutical importance of carbohydrates. Lipids: Chemistry of Fatty acids and Lipids, Classification (Saponifiable and non-saponifiable lipids, Simple, Complex and Derived lipids), Reactions of Fatty acids and other Lipids, Essential fatty acids, Biological and pharmaceutical importance of lipids. Proteins and Amino acids: Chemistry, Classification of proteins and amino acids, Reactions of proteins and amino acids, Organizational levels, Macromolecular nature of proteins, Biological and pharmaceutical importance of proteins and amino acids. Nucleic Acids: Chemistry, Types (DNA, RNA, mRNA, tRNA, rRNA), Purine and Pyrimidine bases, Nucleosides, Nucleotides, Structures of nucleic acids, Biological and pharmaceutical importance of nucleic acids. Vitamins: Chemistry, Classification (Fat-soluble and water-soluble vitamins), Biological and pharmaceutical importance of vitamins. Hormones: Chemistry, Classification (Proteinous and non­proteinous hormones, amino acid derivatives, steroids), Biological and pharmaceutical importance of hormones. Enzymes: Chemistry, Classification, Mode of action, Kinetics (Michaelis Menten Equation and some modifications), Inhibition, Activation, Specificity, Allosteric enzymes, Factors affecting the rate of an enzyme-catalyzed reaction, Biological and pharmaceutical importance, Mechanism of action of some important enzymes (Chymotrypsin, Ribonuclease).

Practical

Hazards and safety in the clinical biochemistry laboratory. Qualitative analysis of: Carbohydrates, amino acids, peptides and proteins, lipids and sterols (cholesterol), bile salts and bilirubin. Analysis of normal and abnormal components of urine including sugar, uric acid, bilirubin, urea and creatinine.

Suggested Reading

1.       Ahmad, M. 2011. Essentials of Medical Biochemistry. Vol. I.  8^th ed. Merit Publishers, Lahore, Pakistan.

2.                   Chatterjea, M.N. and R. Shinde, 2012. Textbook of Medical Biochemistry. 8^th Ed., Jaypee Brothers, Medical Publishers, New Dehli, India.

3.                   Ferrier, D. R. 2013. Biochemistry: Lippincott’s Illustrated Reviews. 6^th ed.  Lippincott Williams and Wilkins, U.S.A.

4.                   Gowenlock, A.H., J.R. McMurray and D.M. McLauchlan, 2006. Varley’s Practical Clinical Biochemistry, 6^th Ed., CBS Publishers and Distributors, New Dehli, India.

5.                   Murray, R.K., D.A. Bender, K. M. Botham, P.J. Kennelly, V.W. Rodwell and P.A.Weil. 2012. Harper’s Illustrated Biochemistry. 29^th ed. McGraw Hill. New York, U.S.A.

6.                   Nelson, D.L and M.M. Cox. 2013. Lehninger Principles of Biochemistry. 6th ed. WH Freeman & Company, New York, N.Y, U.S.A.

7.                   Sood, R., 2005. Medical Laboratory Technology: Methods and Interpretations. 5^th Ed., Jaypee Brothers, Medical Publishers Ltd., New Delhi, India.

Voet, D., Voet, J.G and C.W. Pratt. 2013. Fundamentals of Biochemistry, Life at the Molecular Level. 4^th ed. John Wiley & Sons. Inc. New York. U.S.A.

BIOCHEM-305         PHARMACUETICAL CHEMISTRY-IIB                    4(3-1)

                                    (BIOCHEMISTRY)  

Course Learning Outcomes

By the end of this course students will be able to;

To understand the metabolic pathways and their bioenergetics, their catalysis by enzymes and regulation by different types of hormones and clinical importance of biochemical analysis in diagnosis of different diseases.

Theory

1.METABOLIC FATE OF BIOMOLECULES (Anabolism and Catabolism):

Carbohydrates: Brief introduction to the digestion and absorption of carbohydrates, Aerobic and anaerobic breakdown of Glucose, Glycolysis, Pentose Phosphate Pathway, Glycogenolysis, Glycogenesis, Gluconeogenesis, Citric acid cycle, Energetics of various metabolic processes.

Lipids: Brief introduction to the digestion and absorption of lipids, Oxidation of fatty acids through β-oxidation, Biosynthesis of fatty acids, neutral lipids and cholesterol.

Proteins and Amino acids: Brief introduction to the digestion and absorption of proteins and amino acids, Metabolism of essential and non-essential amino acids, Biosynthesis and catabolism of Haemins and porphyrin compounds.

Bioenergetics: Principles of bioenergetics, Electron transport chain and oxidative phosphorylation.

2. REGULATION OF METABOLIC PROCESSES:  Role of Vitamins: Physiological role of Fat-soluble (A, D, E and K) and Water-soluble (Thiamine, Riboflavin, Pantothenic acid, Niacin, Pyridoxal phosphate, Biotin, Folic acid, Cyanocobalamin-members of B-complex family and Ascorbic acid), Coenzymes and their role in the regulation of metabolic processes. Receptor Mediated regulation (Hormones): Mechanism of action of hormones, Physiological roles of various hormones, Site of synthesis and target sites of hormones. Secondary Messengers: Role of cAMP, Calcium ions and phosphoinositol in the regulation of metabolic processes. Gene Expression: Replication, Transcription and Translation (Gene expression) Introduction to Biotechnology and Genetic Engineering, Basic principles of Recombinant DNA technology, Pharmaceutical applications, Balance of Catabolic, Anabolic and amphibolic processes in human metabolism, Acid-Base and Electrolyte Balance in Human body.

3. INTRODUCTION TO CLINICAL CHEMISTRY:

Introduction and importance of the clinical chemistry. Laboratory tests in diagnosis of diseases including Uric acid, Cholesterol, Bilirubin and Creatinine.

Practical

Estimation of glucose, total proteins and albumin by spectrophotometer, serum minerals, lipid profile (total lipids, triglycerides, total cholesterol, HDL cholesterol, etc). Clinical enzyme: Alanine amino transferase (ALT), aspartate aminotransferase (AST), lactate dehydrogenase (LDH), creatine kinase (CK), alkaline phosphatase. Estimation of vitamin A and C. Units and reference values.

Suggested Readings

1.       Chatterjea, M.N. and R. Shinde, 2012. Textbook of Medical Biochemistry. 8^th Ed., Jaypee Brothers, Medical Publishers, New Dehli, India.

2.                   Ferrier, D. R. 2013. Biochemistry: Lippincott’s Illustrated Reviews. 6^th ed.  Lippincott Williams and Wilkins. U.S.A.

3.                   Gowenlock, A.H., J.R. McMurray and D.M. McLauchlan, 2006. Varley’s Practical Clinical Biochemistry, 6^th Ed., CBS Publishers and Distributors, New Dehli, India.

4.                   Murray, R.K., D.A. Bender, K. M. Botham, P.J. Kennelly, V.W. Rodwell and P.A.Weil. 2012. Harper’s Illustrated Biochemistry. 29^th ed. McGraw Hill. New York, U.S.A.

5.                   Sood, R., 2005. Medical Laboratory Technology: Methods and Interpretations. 5^th Ed., Jaypee Brothers, Medical Publishers Ltd., New Delhi, India.

6.                   Voet, D., Voet, J.G and C.W. Pratt. 2013. Fundamentals of Biochemistry, Life at the Molecular Level. 4^th ed. John Wiley & Sons. Inc. New York, U.S.A.

Proposed/Revised

BIOCHEM-306           INTRODUCTORY BIOCHEMISTRY                 4(3-1)

Course Learning Outcomes

By the end of this course students will be able to;

1. Understand basic knowledge about biomolecules carbohydrates, proteins, lipids and nucleic acids

2. Learn anabolic and catabolic pathways of carbohydrate, lipid, protein and nucleic acids

3. Explain different biochemical assays for the quantitative and qualitative estimation of biomolecules

Theory

Introduction to biochemistry; pH & its importance; Buffer: Henderson-Hasselbalch equation; Carbohydrates: Introduction, classification, glycoside linkages & glycosides isomers, optical activity & rotations, chemical properties of monosaccharide, structure and functions of important monosaccharide, Homopolysaccharide, Heteropolysaccharides; Proteins: Introduction, classification; Structure and classification of amino acids, amphoteric properties of amino acids, concept of Isoelectric pH, peptide linkages; Primary, secondary, tertiary and quaternary structure of proteins; Enzymes: General characteristics and classification, enzyme kinetics; Lipids: Introduction, structure and classification of fatty acids, nomenclature of fatty acid, physical properties of fatty acids and triglycerides, chemical properties of fatty acid  and triglycerides; Sterols and Cholesterol; Prostaglandin and their physical role; Carbohydrate metabolism: Glycolysis, regulation, energy production, Kreb’s Cycle, regulation, energy production, Electron transport chain, pentose phosphate shunt, gluconeogenesis; Protein metabolism: Degradation of proteins and amino acids; Urea cycle and its importance, urea toxicity, regulation of urea cycle; Bioenergetics of protein metabolism; Lipid metabolism: Beta oxidation of even and odd chain fatty acids, biosynthesis of fatty acids, biosynthesis of triglycerides, biosynthesis of cholesterol, biosynthesis of Ketone bodies; DNA metabolism: Biosynthesis and degradation of nucleic acids; Comparative features among animal species of particular relevance, comparative metabolism of mono-gastric and poly-gastric animals.

Practical

Preparation of solutions: Preparation of percentage, molar and normal solutions; Preparation of buffer; Carbohydrate Analysis: Group identification test, Identification of Mono, di and polysaccharides, Identification of reducing sugars, ketose sugar and their confirmation by phenyl hydrazine test, Identification scheme for carbohydrates; Quantitative estimation of glucose in blood sample by glucose oxidase method; Estimation of amino acids by spectrophotometery, Biuret test and ninhydrin test; Precipitation tests of proteins: precipitation of casein at isoelectric point, salt saturation tests, serum protein fractionation by ammonium sulfate precipitation; Separation of the colour pigments of berseen/alfalfa by paper chromatography; Identification of lipids.

Suggested Readings

1. Berg, J.M, L. J. Tymoczko, G.J. Gatto and L. Stryer. 2019. Biochemistry. 9^th Ed. W.H. Freeman and Co., New York, USA

2.       Boyer, R. 2012. Modern Experimental Biochemistry. 4^th Ed. (LPE). Pearson Education, New Delhi, India.

3.       Boyer, R.F. 2000. Modern Experimental Biochemistry. 3^rd Ed. Pearson Education, NJ, USA.

4.       Murray, R., D. Bender, K.M. Botham, P.I. Kennelly, V. Rodwell and P.A. Weil. 2012. Harper’s Issustrated Biochemistry. 29^th Ed. The McGraw-Hill Companies Inc. New York, USA.

5.       Nelson, D.L and M.M. Cox. 2021. Lehninger Principles of Biochemistry. 8^th Ed. WH Freeman & Company, New York, USA.

6.       Nelson, D.L. and M.M. Cox. 2017. Lehninger Principles of Biochemistry. 7^th Ed. W.H. Freeman & Co Ltd., New York, USA.

7.       Nigram, A. and A. Ayyagari. 2007. Lab Manual in Biochemistry, Immunology and Biotechnology. Tata McGraw-Hill Publishing Company Limited, New Dehli, India.

1. Rodwell, V.W., R.K. Murray, D.A. Bender, K.M. Botham, P.J. Kennelly and P.A. Weil. 2021. Harper’s Illustrated Biochemistry. 32^nd Ed. McGraw Hill. New York, USA
2. Stryer, L. 2012. Biochemistry. 7^th Ed. W.H. Freeman and Co., New York, USA

BIOCHEM-401                 GENERAL BIOCHEMISTRY                          4(3-1)

Course Learning Outcomes

By the end of this course students will be able to;

To impart basic knowledge of biomolecules, water and buffer systems and their physiological significance in biological system. To impart practical training of biochemical analysis of biological fluids.

Theory

Introduction, hydrogen ion concentration, ionic product of water. The relationship between pH and pKa, Buffer solutions, Regulation of acid-base balance, functions of acid-base buffers, The Henderson Hasselbalch equation, the buffer systems of body fluids, Respiratory acid base balance, renal regulation of hydrogen ion concentration, renal regulation of hydrogenation concentration, Biomembrane; structures and related processes, transport, passive diffusion, facilitated diffusion, Active transport, Carbohydrates; General characteristics, classification, Stereoisomerisms, Optical Isomerism and optical active, Cyclic forms of sugars, Glycosidic linkage, Chemical properties, Disaccharides, Polysaccharides, Proteins and amino acids; Structure, Amino acids occurring in protein molecules, Peptide linkage, Physiological significance, Classification, Amphoteric properties, Isomerism, Structures Primary, secondary and tertiary, Enzymes; General characteristics, Chemical nature, difference with non-biological catalysts, Activity and unit, Mechanism of enzyme reaction, Coenzymes, Factors effecting enzyme working, Inhibition, Importance in diagnosis, Lipids; Compound lipids, Derived lipids, fatty acids, Saturated and unsaturated with physical and chemical properties, Triglycerides, Properties, Steroids and sterols, Cholesterol, 7-dehydrocholesterol, Ergosterol. Nucleic acids; Chemical composition and structures of DNA and RNA. Functions of DNA and different types of RNA in the cell. Extranuclear DNA and plasmids. Central Dogma and its significance. Introduction to replication, transcription and translation processes.

Practical

Preparation of buffers of definite pH. Determination of pH value of biological fluids. Preparation of solutions of different normalities and molarities and back titration, Qualitative analysis of carbohydrates. Estimation of glucose in biological fluids. Qualitative and quantitative analysis of lipids and proteins. Determination of acid, saponification and iodine values of fats/oils. Estimation of lactose and casein in milk, lipid profiles.

Suggested Reading

1.       Ahmad, M. 2011. Essentials of Medical Biochemistry. Vol. I.  8^th ed. Merit Publishers, Lahore, Pakistan.

2.                   Ferrier, D. R. 2013. Biochemistry: Lippincott’s Illustrated Reviews. 6^th ed.  Lippincott Williams and Wilkins. U.S.A

3.                   Murray, R.K., D.A. Bender, K. M. Botham, P.J. Kennelly, V.W. Rodwell and P.A.Weil. 2012. Harper’s Illustrated Biochemistry. 29^th ed. McGraw Hill. New York,U.S.A.

4.                   Nelson, D.L and M.M. Cox. 2013. Lehninger Principles of Biochemistry. 6th ed. WH Freeman & Company, New York, U.S.A.

5.                   Plummer, D.T. 2009. An Introduction to Practical Biochemistry. 3^rd edition. Tata McGraw-Hill Education (Pvt) Ltd, New Delhi, India.

6.                   Sawhney, S.K. and R. Singh. 2009. Introductory Practical Biochemistry. Narosa Publishing House, New Delhi, India.

BIOCHEM-402/          MOLECULAR BIOLOGY                                         2(2-0)

BIOCHEM-513

Course Learning Outcomes

By the end of this course students will be able to;

1.                   Learn the basic knowledge and concepts of molecular biology.

2.                   Understand the process of DNA replication, DNA damage and repair, transcription and translation.

3.                   Know basic concepts of gene expression and genetic engineering.

Theory

Structural organization of genes and chromosomes in prokaryotes and eukaryotes; Nucleosomes; Properties of DNA and RNA in solution; Nucleic acid stability; DNA Supercoiling; Replication of DNA: Theory, semi-conservative replication and molecular mechanism of replication in prokaryotes and eukaryotes; Enzymology of DNA replication; Molecular nature of mutations, DNA damage and repair; SOS response; Transcription: Promoters and enhancer elements, RNA synthesis in prokaryotes and eukaryotes, tRNA, mRNA and rRNA processing, capping, splicing and polyadenylation of eukaryotic mRNA; Reverse transcription; RNA replication; Genetic code and Wobble hypothesis; Translation, essential factors, enzymes, initiation, elongation and termination of protein synthesis; Post-translational modifications and targeting of proteins; Control of transcription and translation; Regulation of gene expression in prokaryotes; lac and trp operons; Overview of molecular biology techniques; DNA restriction and modification; Advances in biotechnology and genetic engineering. 

Suggested Readings

1.                   Brown, T., 2016. Gene Cloning and DNA Analysis. 7th Ed. Blackwell Scientific Publications, Australia.

2.                                                                      Nelson, D.L. and M.M. Cox. 2021. Lehninger’s Principles of Biochemistry. 8^th Ed. WH Freeman & Company, USA.

3.                   Sambrook, J.F., D.W. Russell and N. Irwin. 2000. Molecular Cloning: A Laboratory Manual. 3^rd Ed. Cold Spring Harbor Laboratory press, New York, USA. 

4.                   Voet, D., Voet, J.G and C.W. Pratt. 2013. Fundamentals of Biochemistry, Life at the Molecular Level. 4^th Ed. John Wiley & Sons. Inc. New York, USA.

5.                   Weaver, R.F. 2012. Molecular Biology. 5^th Ed. McGraw Hill Higher Education, UK.

BIOCHEM-501/                      PLANT BIOCHEMISTRY                             3(3-0)

BIOCHEM-511          

Course Learning Outcomes

By the end of this course students will be able to;

1.                                                                      Describe structure and functions of plant cell and plant cell wall.

2.                                                                      Demonstrate biochemistry of photophosphorylation and its mechanism.

3.                                                                      Use biochemistry of C3 and C4 pathways and secondary metabolites of plants.

4.                                                                      Demonstrate advance knowledge about plant secondary metabolites and vitamins.

Theory

Structure and functions of plant cell; Plant cell wall; Conversion of nitrogen into ammonia and other nitrogenous compounds; Photosynthesis; Structure of chlorophyll, absorption of light energy, photosynthetic pigments, photosystem-1, photosystem-2; Hills reaction: electron transport chain, ATP formation and CO₂ fixation (Calvin Benson cycle); Hatch Slack pathway and photorespiration; Photosynthate translocation; Respiration and lipid metabolism; Secondary metabolites and plant defense: Biosynthesis of alkaloids and their biological functions, terpenes and terpenoids; Plant growth substances; Vitamins: General properties and role in metabolism; Flavonoids and related compounds.

Suggested Readings

1.                   Bowsher, C. and A. Tobin. 2021. Plant Biochemistry. 2^nd Ed. Garland Science, Taylor & Francis, Abingdon, UK.

2.                   Buchanan, B., W. Gruissem and R. Jones. 2015. Biochemistry and Molecular Biology of Plants. John Wiley & Sons. Inc., New York, USA.

3.                   Heldt, H.W. and B. Piechulla. 2021. Plant Biochemistry 5^th Ed. Academic Press, UK. ISBN: 9780128186312 0128186313

4.                   Taiz, L. and E. Zeiger. 2018. Plant Physiology. 6^th Ed. Sinauer Associates, USA.

BIOCHEM-502           FUNDAMENTAL BIOCHEMISTRY                        3(2-1)

Course Learning Outcomes

By the end of this course students will be able to;

To impart fundamental knowledge of structures, functions and metabolic pathways of biomolecules and biochemical analysis of food and plant materials. 

Theory

Carbohydrates: Definition and classification, monosaccharides; pyranose and furanose ring structures. Stereoisomerism and optical isomerism. Glycosidic bond, glycosides. Disaccharides; structures, occurrence and properties. Polysaccharides, structures, occurrence and chemical properties of starch, glycogen and cellulose. Carbohydrate metabolism, respiration, glycolysis, Krebs cycle and fermentation. Electron transport chain. Photosynthesis, energy conversion, carbon fixation, C3, C4 and CAM plant photorespiration. Proteins:  Definition and classification, classification and structures of amino acids, essential and nonessential amino acids. Peptide bond, polypeptide chain and primary, secondary, tertiary and quaternary structures of proteins. Biochemical functions of proteins. Enzymes and co-enzymes. Lipids:  Definition and classification, structures and classification of fatty acids, essential and non-essential fatty acids. Ester formation, simple and mixed triglycerides. Fats and oils; hydrogenation, oxidation and rancidity, β-oxidation of fatty acids. Nucleic Acids:  Structural and functional differences between DNA and RNA. Structur5es of DNA and RNA, Central Dogma and its significance. Fundamentals of DNA replication, transcription and transition.

Practical

Proximate analysis of food/plant materials for moisture, crude protein, crude fibers, ash, ether extract and nitrogen free extract. Determination of true protein and oil contents of plant materials. Estimation of vitamin-C and pectin in fruit juices. Estimation of glucose, fructose and starch in plant products.

Suggested Readings

1.       Boyer, R. 2009. Modern Experimental Biochemistry 3^rd ed (LPE). Pearson Education. New Delhi, India.

2.       Murray, R.K., D.A. Bender, K. M. Botham, P.J. Kennelly, V.W. Rodwell and P.A.Weil. 2012. Harper’s Illustrated Biochemistry. 29^th ed. McGraw Hill. New York.

3.       Nelson, D.L and M.M. Cox. 2013. Lehninger Principles of Biochemistry. 6th ed.

WH Freeman & Company, New York, N.Y,U.S.A.

4.       Sawhney, S.K. and R. Singh. 2009. Introductory Practical Biochemistry. Narosa Publishing House, New Delhi, India.

5.       Shawn, O.F.  and L. E. Taylor. 2009. Biochemistry Lab Manual. Cengage Learning, U.S.A.

6.       Taiz, L. and E. Zeiger. 2010. Plant Physiology. 5^th  ed. Sinauer Associates Inc., U.S.A

Wilson, K. and J. Walker. 2010.  Practical Biochemistry: Principles and Techniques. 7^th ed. Cambridge University Press.

BIOCHEM-503/                      CLINICAL BIOCHEMISTRY                       3(1-2)

  BIOCHEM-515

Course Learning Outcomes

By the end of this course students will be able to;

1.                   Knowledge in the theory and practice of clinical biochemistry as conducted in the modern clinical and health science laboratories.

2.                   Learn about the principle of the tests carried out for biochemical investigations.

3.                   Learn normal ranges and abnormal ranges of biochemical parameters.

4.                   Study about diseases related to biochemical imbalance in human body.

Theory

Laboratory organization and management; Quality control and quality assurance; Biosafety in diagnostic labs; Handling and processing of clinical samples: Specimen collection, preservation and preparation for analysis; Laboratory data processing; Reference range and normal values; Report writing: online tools in report generation; Commonly used instruments in clinical laboratory: Microscope, Biochemistry analyzers, Flame photometer, Hematology analyzers, ELISA.

Practical

Blood sampling techniques; Complete blood picture (CBP); Coagulation profile; Blood grouping; Blood glucose estimation; Serum electrolytes; Liver function tests; Renal function tests; Cardiac function tests; Lipid profile; Urine analysis; Sero-diagnosis of infectious diseases; Visit to clinical laboratory/concerned organization.

Suggested Readings

1.                   Chatterjea, M.N. and R. Shinde. 2012. Text Book of Medical Biochemistry. 8^th Ed. Jaypee Brothers Medical Publishers, New Delhi, India.

2.                   Dacie, J.V. and S.M. Lewis. 2006. Practical Haematology. 10^th Ed. Churchill Livingstone-Elsevier, USA.

3.                   Gaw, A. 2013. Clinical Biochemistry: An Illustrated Colour Text
An Illustrated Colour Text Series. 5^th Ed. Churchill Livingstone, USA.

4.                   Lieberman, M.A. and A. Peet. 2022. Marks’ Basic Medical Biochemistry: A Clinical Approach. 6^th Ed. LWW North American.

5.                   Valley, H. 2021. Practical Clinical Biochemistry. Kindle Edition. CBS Publishers and Distributors Pvt Ltd., India.

6.                   Zia, M.A. 2022. Manual of Clinical Biochemistry. MAS Publishers, Faisalabad, Pakistan.

BIOCHEM-504                       PROTEOMICS                                              3(2-1)

Course Learning Outcomes

By the end of this course students will be able to;

1- learn basic understanding of proteomics

2- learn about different databases of proteomics and their practical importance

3- learn about advance techniques in proteomics such as MALDI and protein microarrays

4- practical training on proteomics using bioinformatics tools

Theory

Introduction to proteomics and protein chemistry; proteome analysis; Bioinformatics analysis: Clustering methods, proteome functional information; Sample Preparation: Protein extraction and quantification; Human proteome Project (HUPO); Techniques in proteomics: iso-electric focusing, two dimensional electrophoresis and analysis, Mass spectrometry; bioinformatics tools for analysis of proteomics data; proteomics database; MS data analysis; peptide mass and fragment fingerprinting; Protein microarrays; Protein sequencing; Protein purification; Immunoproteomics; protein identification; Protein sorting; primary, secondary and tertiary structure prediction; Protein-Protein interactions.

Practical

Searching PubMed; introduction to NCBI; NCBI data bases: BLASTp, PSI-BLAST, Sequence manipulation suite; Multiple sequence alignment; phylogenetic analysis; Software for protein structure prediction using online serves; Protein and protein modelling; Protein structure analysis: ExPasy Server, UniProt, Swiss-Prot, TrEMBL, PROSITE, Predict Protein, ClustalW.

Suggested Readings

1.       Baxevanis, A.D. and B.F.F. Ouellette. 2001. Bioinformatics: A practical guide to the analysis of genes and proteins. John Wiley and Sons, N.Y, U.S.A.

2.       Bourne, P.E. and H. Weissig 2009. Structural Bioinformatics. John Wiley and Sons, N.J.

3.       Buehler, L. K. and H. H. Rashidi. 2005. Bioinformatics Basics: Applications in Biological Science and Medicine. CRC press FL, U.S.A.

4.       Gu, J. and P. E. Bourne. 2009. Structural Bioinformatics, 2^nd Ed., Wiley-Blackwell.

5.       Lesk, A. M. 2008. Introduction to bioinformatics. 3^rd Ed. Oxford Univ. Press, U.K.

6.       Nelson, D.L and M.M. Cox. 2021. Lehninger Principles of Biochemistry. 8th ed. WH Freeman & Company, New York, N.Y, U.S.A.

7.       Richerd S. J. 2004. Purifying Proteins for Proteomics (a laboratory manual) Cord Spring Harbor Laboratory Press.

BIOCHEM-517            Genome Editing: CRISPR Frontiers            3(3-0)

Course Learning Outcomes

By the end of this course students will be able to;

1- Describe basics and history of genome editing

2- Demonstrate advance techniques used in genome editing

2- Apply CRISPR/Cas mediated genome editing in their studies 

Theory

Genome editing: an introduction; Conventional genetic engineering and genome editing: similarities and differences; History of genome editing; Techniques in genome editing: Meganucleases, Zinc Finger Nucleases (ZFNs), Transcription Activator-Like Effector Nucleases (TALENs); Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/CRISPR associated (Cas) system; A brief history of CRISPR/Cas; Mechanism of CRISPR/Cas based genome editing; Components of CRISPR/Cas system: Trans-activating (Tracr-RNA), CRISPR-RNA (crRNA), Post Adjacent Motif (PAM), Cas nuclease; Engineered CRISPR/Cas systems; CRISPR/Cas9: the most widely used CRISPR system for genome editing; Reagents in CRISPR/Cas; Importance of PAM and guide RNA (gRNA); gRNA design tools: CRISPR direct, CHOP CHOP; Off targeting in CRISPR/Cas; Cloning methods in genome editing; Single and multiplex genome editing with CRISPR/Cas; DNA Free Genome Editing; Tracking indels in CRISPR/Cas; Application of CRISPR/Cas in life sciences; Social, ethical and regulatory aspects of CRISPR/Cas edited organisms.

Suggested Readings:

1.                                                                      Doudna, J.A. and S.H. Sternberg. 2017. A Crack in Creation: Gene Editing and the Unthinkable Power to Control Evolution. 1^st edition, Houghton Mifflin Harcourt.

2.                                                                      Ridge, Y. and A. Boersma. 2020. CRISPR: A Powerful Way to Change DNA. 1^st edition, Annick Press; Illustrated edition.

3.                                                                      Lou, Y. 2019. CRISPR Gene Editing, Methods and Protocols. 1^st edition, Humana New York, NY.

4.                                                                      Singh, V. P. Dhar. 2020. Genome Engineering via CRISPR-Cas9 System. 1^st edition, Academic Press.

5.                                                                      Doudna, J. CRISPR-Cas: A Laboratory Manual. 1^st edition, Cold Spring Harbor, New York.

6.                   Ahmad, A., S.H. Khan and Z. Khan. 2022. The CRISPR/Cas Tool Kit for Genome Editing. 1^st edition, Springer Nature.

BIOCHEM-518 The CRISPR/Cas Toolkit for Genome Editing and Beyond       3(3-0)

Course Learning Outcomes

By the end of this course students will be able to;

1- Demonstrate basic and advance knowledge about CRISPR/Cas based genome editing

2- Describe different CRISPR/Cas systems for genome editing

2- Use CRISPR based techniques for genome editing and beyond  

Theory

CRISPR/Cas: a revolutionary genome editing tool; Classification of CRISPR/Cas systems; CRISPR/Cas systems for DNA and RNA editing; Emerging Cas effectors; Bioinformatic tools in CRISPR/Cas; CRISPR Reagents and their delivery methods; Tracking Footprint of Cas nuclease; Expanding CRISPR/Cas techniques:  Gene Knock-out using CRISPR/Cas, Targeted DNA insertion with CRISPR/Cas, Transcriptional regulation with CRISPRi and CRISPRa, RNA editing with Cas13, Cas9 and Cas7-11, Epigenome Editing with CRISPR, CRISPR based genome imaging; Base editing through CRISPR/Cas, Prime Editing; Multiplex Genome Editing, Rewriting of genetic code with CRISPR/Cas, CRISPR meets retrons, CRISPR based gene drives; Off targets and Risks associated with CRISPR/Cas; Global Regulatory Framework of CRISPR edited plants and animals; Social and Ethical Issues of CRISPR/Cas; Global Patent landscape and commercialization of CRISPR/Cas technology; Challenges and opportunities in CRISPR based genome editing.

Suggested Readings:

1.                                                                      Doudna, J.A. and S.H. Sternberg. 2017. A Crack in Creation: Gene Editing and the Unthinkable Power to Control Evolution. 1^st edition, Houghton Mifflin Harcourt.

2.                                                                      Ridge, Y. and A. Boersma. 2020. CRISPR: A Powerful Way to Change DNA. 1^st edition, Annick Press; Illustrated edition.

3.                                                                      Lou, Y. 2019. CRISPR Gene Editing, Methods and Protocols. 1^st edition, Humana New York, NY.

4.                                                                      Singh, V. P. Dhar. 2020. Genome Engineering via CRISPR-Cas9 System. 1^st edition, Academic Press.

5.                                                                      Doudna, J. CRISPR-Cas: A Laboratory Manual. 1^st edition, Cold Spring Harbor, New York.

6.                   Ahmad, A., S.H. Khan and Z. Khan. 2022. The CRISPR/Cas Tool Kit for Genome Editing. 1^st edition, Springer Nature.