Biochemistry II - Molecules 100 Hours Certificate Course (Pre-Medical Program)
Hi there, I am considering in applying for 3 Biochemistry modules online (BSC103, BSC203 and BSC303). Could you please let me know the duration of each module? How many assignments does each module have and how can I do the final exam online? Kind Regards Olga Watson
those modules will require 100 hours of study each to complete.
You can read about the examination process here
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Biochemistry II - Molecules 100 Hours Certificate Course (Pre-Medical Program)
Biochemistry II BSC203 course online. Strengthen your biochemical knowledge and further your career ! Learn about the important building blocks of life including: Amino acids, proteins, sugars, polysaccharides, lipids, enzymes, vitamins, hormones, RNA and DNA.
This course focuses on biochemical molecules. Students would normally have completed Plant or Animal Biochemistry , before attempting this module.
This course is included as a module in the Advanced Diploma in Medical Science (Pre-Medical), which has been endorsed by TQUK - Training Qualifications UK, an Ofqual Approved Awarding Organisation.
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
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
4 Protein Dynamics
- Protein Folding
- Molecular Chaperones
- Heat Shock Proteins: HSP90, HSP70, HSP60, Small Heat Shock Proteins
- The Importance of Understanding Protein Structure
- Structural Evolution of Proteins
- Dynamics of Haem Proteins
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
- Cellular Membranes
7 Enzymes, Vitamins and Hormones
- Enzymes: Coenzymes
- Vitamins: Vitamin Classification, Reviewing Vitamin C
8 DNA and RNA
- Nucleic Acids: Structure of DNA, Types of RNA, Messenger RNA, Transfer RNAs, Ribosomal RNA, Terminology
- DNA Replication
- Interesting Facts about DNA
9 Laboratory Techniques
- Laboratory Health and Safety
- Common Experimental Methods: DNA Methods, Protein Methods, General Methods
- 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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|Course Prerequisite||None - Our course levels are an indication of the depth of learning you should receive. They do not describe the level of difficulty.|
|Course Qualification (Study Option A)||Endorsed Qualification from TQUK - Training Qualifications UK, an Ofqual Approved Awarding Organisation - Completed written assignments, plus final exam (N.B. Some courses have Final Project alternative).|
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|Comparative Credits Information||UK Course Credits: 10 - U.S. Credit Hours: 3 - when compared to regulated courses.|
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