Bachelor of Science (B.Sc) Part 1 Biochemistry syllabus and course input details have been confirmed by Dr. Ram Manohar Lohia Avadh University, Ayodhya.
Introduction to Biochemistry, water as a biological solvent, weak adds and bases, pH, buffers, Henderson-Hasselbalch equation, physiological buffers, fitness of the aqueous environment for living organisms.
Structure of monosaccharides. Stereoisomerism and optical isomerism and sugars Reactions of aldehyde and ketone groups. Ring structure and anomeric forms, mutarotation. Reactions of sugar due to hydroxyl groups. Important derivatives of monosaccharides, disaccharides and trisaccharides (structure, occurrence and functions of important ones). Structure, occurrence and biological importance of monosaccharides, oligosaccharides and polysaccharides e.g. Coliulose, chitin, agar, algenic acids, pectins, pectins, preteolglyague, blood group polysaccharides, glycogen and starch, Bacterial cellwall polysaccharides etc. Glycoproteins.
Definition and classification fatty acids: Introduction classification, nomenclature, structure and properties of saturated and unsaturated fatty acids. Essential fatty acids, prostaglandins. Triacylglycerols: nomenclature, physical properties, chemical properties and characterization of fats – hydrolysis, saponification value, rancidity of fats. Glycophosopholipids (tecithins, lysolecithins, cephalins, phosphatidlyl serine, phosphatidyl inositol, plasmalogens), phospholipids, isoprenoids and sterols.
Introduction, classification based on solubity, shape, composition and functions. Amino acids: common structural features, stereoisomerism and RS system of designating optical isomers, classification and structures of standard amino acids as zwitterion in aqueous solutions, physical and chemical properties, titration of amino acids, separation of amino acids, Essential amino acids.
Peptides: structure of peptide bond, chemical synthesis of polypeptides – protection and deprotection of N-terminal, and C-terminal ends and functional groups in the side-chains, formation of peptide bonds, condensing agents, strategy of chemical synthesis, Merrifield solid-phase peptide synthesis, Determination of the amino acid sequence of a polypeptide chain, specific chemical and enzymatic cleavage of a polypeptide chains and separation of peptides. Protein structure: levels of structure in protein architecture, primary structure of proteins, secondary structure of proteins – helix and pleated sheets, tertiary structure of proteins, forces stabilizing the tertiary structure and quaternary structure of proteins. Denaturation and renaturationo of proteins. Behaviour of proteins in solutions, salting in and salting out of proteins. Structure and biological functions of fibrous proteins (keratins, collagen and elastin), globular proteins (hemoglobin, myoglobin), lipoproteins, metalloproteins, glycoproteins and nucleoproteins.
Porphyrins: Porphyrin nucleus and classification of porphyrins. Important Metalloporphyrins occurring in nature. Detection of porphyrins spectrophotometrically and by fluorescence. Bile pigments – chemical nature and their physiological significance.
Principles of thermodynamics and their applications in biochemistry introduction, thermodynamic system, thermodynamic state functions, first and second laws of thermodynamics, concept of free energy, standard free energy, determination of Δ G for a reaction relation between equilibrium constant and standard free energy change, biological standard state and standard free energy change in coupled reactions. Biological oxidation-reduction reactions – introduction, redox potentials, relation between standard reduction potentials and free energy change (derivations and numerical included). High-energy phosphate compounds – introduction, phosphate group transfers-free energy of hydrolysis of ATP and sugar phosphates along with reasons for his Δ G.
Sedimentation – sedimentation velocity, preparative and analytical ultracentrifugation techniques, determination of molecular weight by hydrodynamic methods (derivations excluded and numerical included).
Principles of glass and reference electrodes, types of electrodes, complications of pH measurement (dependence of pH on ionic strength, electrode contamination and sodium error) and use of pH paper.
Types of radioisotopes used in Biochemistry, units of radioactivity measurements, techniques used to measure radioactivity (gas ionization and liquid scintillation counting), nuclear emulsions used in biological studies (pro-mounted, liquid and stripping), isotopes commonly used in biochemical studies – 32P, 35S, 14C and 3H), Autoradiography, Biological hazards 4 radiation and safety measures in handling radioisotopes, Biological, applications.
General principles and applications of:
Basic principles of agarose electrophoresis, PAGE and SDS-PAGE, Two-dimensional electrophoresis, its importance, isoelectrofocussing.
Beer-Lambert Law, light absorption and its transmittance, determination and application of extinction coefficient, application of visible and UV spectroscopic techniques (structure elucidation and numerical excluded). Principle and application of NMR, ESR, Mass spectroscopy, Fluorescent and emission spectroscopy.
Immunodiffusion, immunoelectrophoresis, radiomimmunoassay, ELISA immunoffuorescence.
Cell size, shape, comparison of prokaryotic and eukaryotic cell structure, cell types including cellular specialization and differentiation, differences in plant and animal cells, Photosynthesis and Nitrogen metabolism.
Detailed description of eukaryotic cell structure, endoplasmic reticulum, nucleus, mitochondria, lysosomes, peroxisomes, Golgi apparatus, ribosomes and polysomes, cytoskeletal elements.
Use of light microscopy, phase contrast microscopy, transmission and scanning electror, microscopy, electron tunneling microscopy and freeze fracture technique in the study of cells and cell organelles.
Cell cycle and Cell growth, Cell and tissue culture techniques, properties of cell in culture.
Types and sub cellular location. Chemical composition of biomemranes, Gap and tight junctions. Model lipid membranes – preparation and properties, similarities and differences between biomembranes and artificial phospholipid membranes. Physical and biochemical methods to study membrane structure and properties, different models of cell membrane – a historical perspective, Functions of biomembranes with examples-energy transduction, signal recognition. Specialized forms or membranes-brush border, flagella and pancreatic activity.
Nutrient transport across biomembranes. Simple diffusion and Fick’s law. Porins facilitated diffusion. Porter molecules, Kinetics of facilitated transport. Sympor, antiportand uiport. Red cell membrane-proteins. Anion porter and glucose porter. Active transport, Proton and Na+-K+ pumps – examples and metabolic significance.
Structure and functions. Methods to study membrane receptors. Purification and characterization of adrenergic and cholinergic receptors.
Structure, composition and biosynethesis. Inhibitors of cell wall synthesis.
Download RMLAU B.Sc Biochemistry 1st year syllabus here in PDF: http://rmlau.ac.in/pdf/julbiochem11.pdf
| B.Sc Biochemistry 1st Year Syllabus of Avadh University: |
| Paper | Name of the Paper | Maximum Marks |
|---|---|---|
| BBC 101 | Biomolecules | 45 |
| BBC 102 | Biophysical and Biochemical Techniques | 45 |
| BBC 103 | Cell Biology and Membrane Biochemistry | 45 |
| BBC 104 | Laboratory Course I | 60 |
| Paper – I (Biomolecules) of RMLAU B.Sc Biochemistry Part 1 Syllabus (BBC - 101): |
| Introduction: |
Introduction to Biochemistry, water as a biological solvent, weak adds and bases, pH, buffers, Henderson-Hasselbalch equation, physiological buffers, fitness of the aqueous environment for living organisms.
| (i) Carbohydrates |
Structure of monosaccharides. Stereoisomerism and optical isomerism and sugars Reactions of aldehyde and ketone groups. Ring structure and anomeric forms, mutarotation. Reactions of sugar due to hydroxyl groups. Important derivatives of monosaccharides, disaccharides and trisaccharides (structure, occurrence and functions of important ones). Structure, occurrence and biological importance of monosaccharides, oligosaccharides and polysaccharides e.g. Coliulose, chitin, agar, algenic acids, pectins, pectins, preteolglyague, blood group polysaccharides, glycogen and starch, Bacterial cellwall polysaccharides etc. Glycoproteins.
| (ii) Lipids |
Definition and classification fatty acids: Introduction classification, nomenclature, structure and properties of saturated and unsaturated fatty acids. Essential fatty acids, prostaglandins. Triacylglycerols: nomenclature, physical properties, chemical properties and characterization of fats – hydrolysis, saponification value, rancidity of fats. Glycophosopholipids (tecithins, lysolecithins, cephalins, phosphatidlyl serine, phosphatidyl inositol, plasmalogens), phospholipids, isoprenoids and sterols.
| (iii) Proteins |
Introduction, classification based on solubity, shape, composition and functions. Amino acids: common structural features, stereoisomerism and RS system of designating optical isomers, classification and structures of standard amino acids as zwitterion in aqueous solutions, physical and chemical properties, titration of amino acids, separation of amino acids, Essential amino acids.
Peptides: structure of peptide bond, chemical synthesis of polypeptides – protection and deprotection of N-terminal, and C-terminal ends and functional groups in the side-chains, formation of peptide bonds, condensing agents, strategy of chemical synthesis, Merrifield solid-phase peptide synthesis, Determination of the amino acid sequence of a polypeptide chain, specific chemical and enzymatic cleavage of a polypeptide chains and separation of peptides. Protein structure: levels of structure in protein architecture, primary structure of proteins, secondary structure of proteins – helix and pleated sheets, tertiary structure of proteins, forces stabilizing the tertiary structure and quaternary structure of proteins. Denaturation and renaturationo of proteins. Behaviour of proteins in solutions, salting in and salting out of proteins. Structure and biological functions of fibrous proteins (keratins, collagen and elastin), globular proteins (hemoglobin, myoglobin), lipoproteins, metalloproteins, glycoproteins and nucleoproteins.
| (iv) Porphyrlns: |
Porphyrins: Porphyrin nucleus and classification of porphyrins. Important Metalloporphyrins occurring in nature. Detection of porphyrins spectrophotometrically and by fluorescence. Bile pigments – chemical nature and their physiological significance.
| Paper – II (Biophysical and Biochemical Techniques) of RMLAU Faizabad B.Sc Biochemistry Part 1 Syllabus (BBC - 102): |
| (i) Concepts of Bioenergetics |
Principles of thermodynamics and their applications in biochemistry introduction, thermodynamic system, thermodynamic state functions, first and second laws of thermodynamics, concept of free energy, standard free energy, determination of Δ G for a reaction relation between equilibrium constant and standard free energy change, biological standard state and standard free energy change in coupled reactions. Biological oxidation-reduction reactions – introduction, redox potentials, relation between standard reduction potentials and free energy change (derivations and numerical included). High-energy phosphate compounds – introduction, phosphate group transfers-free energy of hydrolysis of ATP and sugar phosphates along with reasons for his Δ G.
| (ii) Hydrodynamic Methods |
Sedimentation – sedimentation velocity, preparative and analytical ultracentrifugation techniques, determination of molecular weight by hydrodynamic methods (derivations excluded and numerical included).
| (iii) Measurement of pH |
Principles of glass and reference electrodes, types of electrodes, complications of pH measurement (dependence of pH on ionic strength, electrode contamination and sodium error) and use of pH paper.
| (iv) Radioisotopic Techniques |
Types of radioisotopes used in Biochemistry, units of radioactivity measurements, techniques used to measure radioactivity (gas ionization and liquid scintillation counting), nuclear emulsions used in biological studies (pro-mounted, liquid and stripping), isotopes commonly used in biochemical studies – 32P, 35S, 14C and 3H), Autoradiography, Biological hazards 4 radiation and safety measures in handling radioisotopes, Biological, applications.
| (v) Chromatography |
General principles and applications of:
- Adsorption chromatography
- Ion-exchange chromatography
- Thin-layer chromatography
- Molecular-sieve chromatography
- Hydrophobic chromatography
- Gas-liquid chromatography
- HPLC
- Affinity chromatography
- Paper chromatography
| (vi) Electrophoresis |
Basic principles of agarose electrophoresis, PAGE and SDS-PAGE, Two-dimensional electrophoresis, its importance, isoelectrofocussing.
| (vii) Spectroscopic Techniques |
Beer-Lambert Law, light absorption and its transmittance, determination and application of extinction coefficient, application of visible and UV spectroscopic techniques (structure elucidation and numerical excluded). Principle and application of NMR, ESR, Mass spectroscopy, Fluorescent and emission spectroscopy.
| (viii) Immunological Techniques |
Immunodiffusion, immunoelectrophoresis, radiomimmunoassay, ELISA immunoffuorescence.
| Paper – III (Cell Biology and Membrane Biochemistry) of Faizabad University B.Sc Biochemistry Part 1 Syllabus (BBC - 103): |
| A. Cell Biology |
| (i) Morphology of Cell |
Cell size, shape, comparison of prokaryotic and eukaryotic cell structure, cell types including cellular specialization and differentiation, differences in plant and animal cells, Photosynthesis and Nitrogen metabolism.
| (ii) Structure and Function of Cell Organelles |
Detailed description of eukaryotic cell structure, endoplasmic reticulum, nucleus, mitochondria, lysosomes, peroxisomes, Golgi apparatus, ribosomes and polysomes, cytoskeletal elements.
| (iii) Cell biology Techniques |
Use of light microscopy, phase contrast microscopy, transmission and scanning electror, microscopy, electron tunneling microscopy and freeze fracture technique in the study of cells and cell organelles.
| (iv) Cell Division |
Cell cycle and Cell growth, Cell and tissue culture techniques, properties of cell in culture.
| B. Membrane Biochemistry |
| (i) Biological Membranes |
Types and sub cellular location. Chemical composition of biomemranes, Gap and tight junctions. Model lipid membranes – preparation and properties, similarities and differences between biomembranes and artificial phospholipid membranes. Physical and biochemical methods to study membrane structure and properties, different models of cell membrane – a historical perspective, Functions of biomembranes with examples-energy transduction, signal recognition. Specialized forms or membranes-brush border, flagella and pancreatic activity.
| (ii) Membrane Transport |
Nutrient transport across biomembranes. Simple diffusion and Fick’s law. Porins facilitated diffusion. Porter molecules, Kinetics of facilitated transport. Sympor, antiportand uiport. Red cell membrane-proteins. Anion porter and glucose porter. Active transport, Proton and Na+-K+ pumps – examples and metabolic significance.
| (iii) Membrane Receptors |
Structure and functions. Methods to study membrane receptors. Purification and characterization of adrenergic and cholinergic receptors.
| (iv) Bacterial and Plant cell walls |
Structure, composition and biosynethesis. Inhibitors of cell wall synthesis.
| BBC 104 Practical for 1st Year Laboratory – I |
| 1. Preparation of standard buffers and determination of pH of a solution |
| 2. Qualitative tests for: |
| a) Carbohydrates |
| b) Proteins and amino acids |
| c) Lipids |
| 3. Determination of saponification value and iodine number of fats |
| 4. Estimation of ascorbic acid |
| 5. Titration curve for amino acids and determination of pH value |
| 6. Verification of Beer-Lambert’s law |
| 7. Estimation of |
| (i) Carbohydrate by anthrone method |
| (ii) Blood glucose by the methods (a) Folin-Wu (b) Nelson-Somogyi |
| 8. Estimation of amino acids by ninhydrin method |
| 9. Isolation and assay of glycogen from rat liver |
| 10. (i) Extraction of total lipids by Folch method |
| (ii) Estimation of food adulterant |
| 11. Estimation of DNA and RNA |
| 12. Separation of Sugars using paper chromatography |
Download RMLAU B.Sc Biochemistry 1st year syllabus here in PDF: http://rmlau.ac.in/pdf/julbiochem11.pdf
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