Biochemistry II (Molecules) (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) (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.The Advanced Diploma has also been approved by the Royal College of Surgeons in Bahrain, Ireland and Malaysia, meaning that the qualification can be used to support an application to attend Medical School in these countries (subject to applicants satisfying their other entrance criteria). It is also accepted by other universities around the world.
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.
|Recognised Issuing Body||TQUK - Training Qualifications UK, an Ofqual Approved Awarding Organisation.|
|Course Prerequisite||No, start at anytime|
|Course Qualification||Level 4. This course may be studied as a stand alone course or in conjunction with the Advanced Diploma in Medical Science.|
|Exam Required?||Finalised with an exam/test|
|UK Course Credits||10 Credits|
|US Course Credit Hours||3 Credit Hours|
|Study Support||You'll be allocated your own personal tutor/mentor who will support and mentor you throughout your whole course. Our tutors/mentors have been specifically chosen for their business expertise, qualifications and must be active within their industry. Tutors are contactable by e-mail, telephone and through our Moodle Student Support Zone online. Tutors are there to provide assistance with course material, discuss, explain and give advice and support throughout the whole programme. Their feedback is vital to your success.|
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