Lesson Structure:  Biochemistry II BSC203

There are 9 lessons:

1  Introduction to Biochemical Molecules

• What is Biochemistry?
• Cells: Prokaryote Cells, Eukaryote Cells, Viruses and Prions
• Biomolecules: Proteins, Carbohydrates, Lipids, Nucleic Acids, Vitamins and Co-enzymes, Hormones and Neurotransmitters
• Metabolic Processes: Catabolism, Anabolism

2  Amino Acids

• Amino Acids: Biochemical Nomenclature   
• Amino Acid Properties: Acidic and Basic, Hydrophilic and Hydrophobic, Polarity of the Side Chain, Amino Acid Polarity, Non standard Amino Acids
• Genetic Coding of Amino Acids: Terminology

3  Structure of Proteins

• Proteins: Protein Functions, Primary Structure, Secondary Structure, Tertiary Structure, Quaternary Structure
• What are Fibrous Proteins? Collagen, Elastin, Keratin, Globular Proteins, Albumin
• Cofactors and Conformation
• Post-Translational Modifications
• Protein Denaturation
• Protein Degredation
• Terminology

4  Protein Dynamics

• Protein Folding
• Molecular Chaperones
• Heat Shock Proteins: HSP90, HSP70, HSP60, Small Heat Shock Proteins
• Chaperones
• The Importance of Understanding Protein Structure
• Structural Evolution of Proteins
• Dynamics of Haem Proteins
• Terminology

5  Sugars and Polysaccharides

• Saccharides: Monosaccharides, Oligosaccharides, Polysaccharides, Lectins
• Polysaccharide Bonds
• Polysaccharide Function
• Classification of Monosaccharides: Ring or Chain Types
• Complex Sugars: Monosaccharides, Disaccharides, Polysaccharides, Cellulose

6  Lipids (Fats) and Membranes

• Lipids: Fatty Acids, Tryacilglicerols, Neutral Lipids, Phospholipids, Glycolipids, Terpenoids
• Cholestrol
• Cellular Membranes
• Terminology

7  Enzymes, Vitamins and Hormones

• Enzymes: Coenzymes
• Vitamins: Vitamin Classification, Reviewing Vitamin C
• Hormones

8  DNA and RNA

• Nucleic Acids: Structure of DNA, Types of RNA, Messenger RNA, Transfer RNAs, Ribosomal RNA, Terminology
• DNA Replication
• Inheritance
• Interesting Facts about DNA

9  Laboratory Techniques

• Laboratory Health and Safety
• Common Experimental Methods: DNA Methods, Protein Methods, General Methods  

Learning Goals:   Biochemistry II BSC203

• Learn the characteristics of biochemical molecules and to distinguish between different groups of biochemical molecules
• Describe the structural characteristics and other properties that differentiate standard amino acids one from another
• Learn about the structures of different proteins (both covalent and 3-dimensional)
• Describe common protein dynamics including folding, structural evolution and haemoglobin function
• Describe the structure and dynamics of different types of saccharides and polysaccharides
• Understand the composition and structure of both lipids and membranes
• Describe the structure and dynamics of different types of enzymes, vitamins and hormones
• Describe the structure and function of different types of nucleic acids including DNA and RNA
• Become familiar with some of the basic laboratory techniques used in biochemistry and to appreciate the importance of safety in the laboratory

Practicals:

• Describe some of the main differences between prokaryote and eukaryote cells
• Explain mitochondria and why are they important for cellular functioning in eukaryotes
• Explain the difference between dextrorotary and levorotary molecules
• Explain the difference between standard and non-standard amino acids
• Name the bond that is created between two adjacent amino acids in a chain, and state what two chemical groups are involved in forming this bond
• Name some of the methods used today to determine the amino acid sequence of a polypeptide
• State common causes of protein denaturation
• Explain why sickle cell anaemia is called a 'molecular disease'
• List the main types of secondary structure present in proteins and the structural categories of proteinsInclude examples
• Name the bond that can form between cysteine residues in a polypeptide and explain why these are important
• Explain why polypeptide or protein folding is important
• Comment on the statement that 'proteins and enzymes have static structures'
• Describe what might be required for a protein to fold efficiently into its active (or native) conformation
• Define polysaccharides
• Name one polysaccharide important in nature and describe its structure
  • Explain glycoproteins
  • Classify lipids
• Explain why fats are an efficient form of energy storage
• Draw a saturated and non-saturated hydrocarbon
• State what class of biomolecules enzymes belong to
• Explain the role of enzymes in metabolism
• Explain how the flux of reactants through metabolic pathways can be controlled via enzyme regulation
• Do an Internet search to find out information on the structure of DNA proposed by Watson and Crick in 1953Discuss the significance of their findings
• Name the four nucleotide bases that DNA is composed of and state which bases can pair with each other on opposite strands.
• Describe the structure of DNA (B-DNA) with as many of the essential features as you can list.
• Describe the equipment used for gel and paper electrophoresis and the operation principles.
• List some methods for purifying and studying proteins along with a brief description of each method.
• List some of the properties of proteins that form the basis for their purification and separation from each other.

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Here is a list of the most often asked FAQ’s.

General

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