Week 2 - Proteins & Enzymes
- Identify the structure and bonding in a generic amino acid
- Describe the four structural levels of a protein
- Recall the process of protein synthesis (this is going to be covered in week three)
- Describe the process of enzyme-substrate interaction
- Recollect factors that influence the rate of an enzymatic reaction:
- Enzyme Concentration
- Substrate Concentration
Name the major classes of enzyme and give examples of each
Additional questions to support your studies.
- Draw an a typical amino acid and label the groups. Describe and name the potential polarity of this molecule and describe the importance of this.
- Draw the formation of a di-peptide between the amino acids glycine and cystine.
- Give examples of hydrophobic, hydrophilic, acidic and basic amino acids and comment on how the polarity of a side group can help to confer the structure of a protein.
- What is an essential amino acid? Give examples.
- Using diagrams to explain your answer describe the structure of a ‘general’ protein. What types of bonds are required to form this structure? Give examples.
- Proteins are multifunctional. Give examples of the diverse range of protein function.
- What is an enzyme? Why are they biologically important? How do they affect the activation energy of a reaction? (Hint- a graph my help).
- Compare and contrast competitive and non-competitive enzyme inhibition.
- What is a VMAX? What is a KM? How can these be calculated?
- What external factors affect the rate of an enzymatic reaction? Give examples. There are 6 classes of enzyme. Name and give examples from each group.
Complete Cardiac Transplant. (Warning: Graphic and not safe for work)