Biochemistry II (Molecules) BSC203 (Pre-Medical Program)
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In this unique situation, I will acknowledge on the off chance that you could mercifully send the endorsements for the courses (duplicate via email until further notice) I have finished with ADL so I can present to my new manager. Saying thanks to you ahead of time and sitting tight for the joy to get notification from you soon.
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I attended this module the previous summer as I expected to cover the prerequisite to be acknowledged into a Biomedical Science Degree course. I figured out how to finish the coursework and exam for Biochemistry I and III modules in a little more than two months(200h learning time). My guide was extraordinary, I addressed her initially and disclosed I expected to work at a truly quick pace. She participated and elucidated my questions at whatever point I required it. On the whole, I had a better than average experience contemplating with ADL. While doing distance learning study, you truly need to center and be trained, yet it is all justified, despite all the trouble toward the end. I was acknowledged into my course, I have finished my first year and going to begin the second one. Much obliged to you ADL and my guide Juliette Ivanova for your support
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Vocational qualification
Distance
£ 340
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Open Learning College
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City College Norwich
Course OnlinePrice on request -
Canterbury College
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ICS
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Thompson Rivers University
Course OnlinePrice on request -
George Washington University
Bachelor's degree OnlinePrice on request -
Oxford Open Learning
GCSE Distance Learning£ 295 + VAT
Description
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Type
Vocational qualification
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Methodology
Distance Learning
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Start date
Different dates available
Prices from May 1st - Save money by enrolling now
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.None
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Location
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Distance Learning
Start date
Different dates availableEnrolment now open
Reviews
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In this unique situation, I will acknowledge on the off chance that you could mercifully send the endorsements for the courses (duplicate via email until further notice) I have finished with ADL so I can present to my new manager. Saying thanks to you ahead of time and sitting tight for the joy to get notification from you soon.
← | →
-
I attended this module the previous summer as I expected to cover the prerequisite to be acknowledged into a Biomedical Science Degree course. I figured out how to finish the coursework and exam for Biochemistry I and III modules in a little more than two months(200h learning time). My guide was extraordinary, I addressed her initially and disclosed I expected to work at a truly quick pace. She participated and elucidated my questions at whatever point I required it. On the whole, I had a better than average experience contemplating with ADL. While doing distance learning study, you truly need to center and be trained, yet it is all justified, despite all the trouble toward the end. I was acknowledged into my course, I have finished my first year and going to begin the second one. Much obliged to you ADL and my guide Juliette Ivanova for your support
← | →
100%
Course rating
Recommended
Centre rating
Have you taken this course?
Leckraz K.
What I would highlight:
In this unique situation, I will acknowledge on the off chance that you could mercifully send the endorsements for the courses (duplicate via email until further notice) I have finished with ADL so I can present to my new manager. Saying thanks to you ahead of time and sitting tight for the joy to get notification from you soon.
What could be improved:
Nothing.
Would you recommend this course?:
Yes
Maria R.
What I would highlight:
I attended this module the previous summer as I expected to cover the prerequisite to be acknowledged into a Biomedical Science Degree course. I figured out how to finish the coursework and exam for Biochemistry I and III modules in a little more than two months(200h learning time). My guide was extraordinary, I addressed her initially and disclosed I expected to work at a truly quick pace. She participated and elucidated my questions at whatever point I required it. On the whole, I had a better than average experience contemplating with ADL. While doing distance learning study, you truly need to center and be trained, yet it is all justified, despite all the trouble toward the end. I was acknowledged into my course, I have finished my first year and going to begin the second one. Much obliged to you ADL and my guide Juliette Ivanova for your support
What could be improved:
Nothing.
Would you recommend this course?:
Yes
This centre's achievements
2017
All courses are up to date
The average rating is higher than 3.7
More than 50 reviews in the last 12 months
This centre has featured on Emagister for 15 years
Subjects
- 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
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
Additional information
Medicine and Research
ASIQUAL
ASIQUAL
Biochemistry II (Molecules) BSC203 (Pre-Medical Program)
£ 340
+ VAT
-
Open Learning College
Course Distance Learning£ 400 £ 518 -
City College Norwich
Course OnlinePrice on request -
Canterbury College
BTEC OnlinePrice on request -
ICS
Course Online£ 285 -
Thompson Rivers University
Course OnlinePrice on request -
George Washington University
Bachelor's degree OnlinePrice on request -
Oxford Open Learning
GCSE Distance Learning£ 295 + VAT