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M5)Protein Structure
Proteins' 3D structure is critical to its function.
| Question | Answer |
|---|---|
| What are the levels of protein structure? | Primary, secondary, tertiary and quaternary |
| What is primary structure? | The specific type and sequence of amino acids. |
| What is secondary structure? | The coiling or folding of the polypeptide chain, caused by hydrogen bonding,into a coil, fibril or pleated sheet pattern. |
| What is tertiary structure? | The 3D shape of the polypeptide that forms spontaneously from attractions and repulsions between amino acids. Very important for globular proteins. |
| What is quaternary structure? | In proteins that have 2 or more polypeptide chains, the bonding between them. |
| What is haemoglobin? | A protein which carries oxygen in the blood. It has 2 pairs of polypeptide chains and about 600 amino acids. |
| What are the functions of proteins in the cell membrane? | Receptors for inter-cellular chemical messages, and one-way transport channels that allow specific molecules in and out. |
| What is an example of a specific messenger molecule? | Hormone. |
| What are enzymes? | Biological catalysts that speed up reactions in cells and are usually proteins. They are not used up. |
| What determines the specificity of the enzyme? | Its 3D shape. |
| What are the substances that enzymes bind to? | Substrate molecules. |
| What are antibodies? | Protein molecules that are a part of organisms' defence systems. They act by binding to antigens. |
| What enables antibodies to bind to antigens? | Their specific 3D complementary shape. (quaternary) |