Biochemistry II (Molecules) BSC203 (Pre-Medical Program)

ADL - Academy for Distance Learning
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£ 325 - (Rs 28,168)
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Important information

  • Vocational qualification
  • Distance learning
  • When:
    Flexible
Description

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.
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Where and when

Starts Location
Flexible
Distance Learning

What you'll learn on the course

Basic
Internet
Basic IT training
Basic IT
Secondary
Composition
Biochemistry
Medical
Medical training
Biomedical Sciences, Medicine, Research

Course programme

Lesson Structure: Biochemistry II BSC203

Introduction to Biochemical Molecules
Amino Acids
Structure of Proteins
Protein Dynamics
Sugars and Polysaccharides
Lipids (Fats) and Membranes
Enzymes, Vitamins and Hormones
DNA and RNA
Laboratory Techniques
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.Lesson Structure: Biochemistry II BSC203

Introduction to Biochemical Molecules
Amino Acids
Structure of Proteins
Protein Dynamics
Sugars and Polysaccharides
Lipids (Fats) and Membranes
Enzymes, Vitamins and Hormones
DNA and RNA
Laboratory Techniques
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.Lesson Structure: Biochemistry II BSC203

Introduction to Biochemical Molecules
Amino Acids
Structure of Proteins
Protein Dynamics
Sugars and Polysaccharides
Lipids (Fats) and Membranes
Enzymes, Vitamins and Hormones
DNA and RNA
Laboratory Techniques
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.Lesson Structure: Biochemistry II BSC203

Introduction to Biochemical Molecules
Amino Acids
Structure of Proteins
Protein Dynamics
Sugars and Polysaccharides
Lipids (Fats) and Membranes
Enzymes, Vitamins and Hormones
DNA and RNA
Laboratory Techniques
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.Lesson Structure: Biochemistry II BSC203

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Medicine and Research
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