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Syllabus

2.4 Proteins

Path:

Core » Topic 2: Molecular biology » 2.4 Proteins

Description

Nature of science:
Looking for patterns, trends and discrepancies—most but not all organisms assemble proteins from the same amino acids. (3.1)

Understandings:

Amino acids are linked together by condensation to form polypeptides.
There are 20 different amino acids in polypeptides synthesized on ribosomes.
Amino acids can be linked together in any sequence giving a huge range of possible polypeptides.
The amino acid sequence of polypeptides is coded for by genes.
A protein may consist of a single polypeptide or more than one polypeptide linked together.
The amino acid sequence determines the three-dimensional conformation of a protein.
Living organisms synthesize many different proteins with a wide range of functions.
Every individual has a unique proteome.

Applications and skills:

Application: Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of protein functions.
Application: Denaturation of proteins by heat or by deviation of pH from the optimum.
Skill: Drawing molecular diagrams to show the formation of a peptide bond.

Guidance:

The detailed structure of the six proteins selected to illustrate the functions of proteins is not needed.
Egg white or albumin solutions can be used in denaturation experiments.
Students should know that most organisms use the same 20 amino acids in the same genetic code although there are some exceptions. Specific examples could be used for illustration.

Utilization:

Proteomics and the production of proteins by cells cultured in fermenters offer many opportunities for the food, pharmaceutical and other industries.

Aims:

Aim 7: ICT can be used for molecular visualization of the structure of proteins.
Aim 8: Obtaining samples of human blood for immunological, pharmaceutical and anthropological studies is an international endeavour with many ethical issues.

Directly related questions

17N.1.HL.TZ0.05: Which of the molecules contain peptide bonds or are sugar molecules?
17N.1.SL.TZ0.06: Which molecule could be hydrolysed into amino acids?
17M.3.SL.TZ2.2c: State two conditions that should be kept constant in both experiments.
17M.3.SL.TZ2.2b: Suggest two changes occurring in the reaction vessel that could be used to indicate keratinase...
17M.3.SL.TZ2.2a: Determine the optimum pH and temperature of keratinase.
17M.2.HL.TZ1.6a: Describe the functioning of immunoglobulins.
17M.2.HL.TZ1.1f.ii: Suggest a reason for the greater expression of the gene for the urea transporter after an...
17M.2.SL.TZ2.5a: Draw a molecular diagram of an amino acid to show its general structure.
17M.2.SL.TZ1.1c: Estimate how much smaller drilled oysters raised in seawater at a high CO2 concentration were...
17M.1.SL.TZ2.27: The bacterium Neisseria gonorrhoeae causes infections related to the human reproductive system....
17M.1.SL.TZ1.9: The most abundant structural protein in the human body is found in ligaments and skin. What is...
17M.1.SL.TZ1.21: Cladograms can be created by comparing DNA or protein sequences. The cladogram on the left is...
17M.1.SL.TZ1.15: How does the proteome of a species contain a larger number of proteins than genes that code for...
16N.1.SL.TZ0.7: The diagram shows a molecular structure. Which type of molecule is shown? A. Amino acidB....
16M.1.SL.TZ0.3: Which is an effect of protein denaturation? A. The order of amino acids is changed when the...
15M.1.SL.TZ2.9: The image shows the structural formula of a molecule. What is this molecule?A. Amino acidB....
15M.1.HL.TZ2.6: Where are proteins synthesized by free ribosomes used? A. Outside the cell after secretionB....
15M.1.SL.TZ1.8: What are these molecules?
15N.2.SL.TZ0.6c: Outline the production of a dipeptide by a condensation reaction, showing the structure of a...
13M.1.HL.TZ1.26: A channel protein is used to transport ions across a membrane. What would you expect to find...
13N.2.HL.TZ0.8a: Outline the role of condensation and hydrolysis in the relationship between amino acids and...
13M.3.SL.TZ2.8a: Transport is the function of the protein known as hemoglobin. State the name and function of...
13N.3.SL.TZ0.8a.i: Other than acting as catalysts state three functions of proteins, giving an example of each.
11M.1.HL.TZ1.7: Which type of molecule is shown in the diagram below? A. PeptideB. CarbohydrateC. LipidD....
11M.1.SL.TZ2.14: How many molecules of water are required to completely hydrolyse a polypeptide made up of 23...
11M.3.SL.TZ1.2c: Amino acid polarity is an important factor in determining the functions of proteins. Explain the...
12M.2.HL.TZ2.5a: List the general functions of non-membrane proteins.
12M.2.SL.TZ2.6c: Discuss the relationship between one gene and one polypeptide.
10M.2.HL.TZ2.5b: Distinguish between fibrous and globular proteins with reference to one example of each protein...
10M.1.SL.TZ1.7: Which substance in prokaryotes contains sulfur? A. DNA B. Phospholipids C. Proteins D. Antibiotics
10M.1.SL.TZ2.7: What is a role of sulfur in living organisms? A. Formation of proteins B. Formation of...
10M.3.SL.TZ1.10a: State two functions of proteins, giving a named example of each.
10M.3.SL.TZ2.9a: List three functions of proteins, giving a named example of each.
11N.1.HL.TZ0.6: Which molecular structure correctly illustrates two amino acids linked by a peptide bond?
12N.2.HL.TZ0.1f: Using all the data provided, evaluate the hypothesis that the presence of proteins in surfactants...
10N.2.SL.TZ0.4a: State four elements that are needed by living organisms, other than carbon, hydrogen and oxygen,...
10N.2.HL.TZ0.4a: State four functions of proteins, giving a named example of each.

Sub sections and their related questions

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