Biochemistry: Proteins & Enzymes
Biochemistry: Proteins & Enzymes
💡 Key Takeaways
- Understand how a protein's amino acid sequence and folding determine its structure from primary to quaternary and its function.
- Learn how enzymes act as biological catalysts, including active sites, substrate specificity, and the induced-fit model.
- Describe factors that influence enzyme activity (temperature, pH, substrate concentration) and common regulatory mechanisms or inhibitors.
- Get a basic grasp of enzyme kinetics concepts (Vmax, Km) and how inhibitors affect reaction rates.
❓ Frequently Asked Questions
What are proteins and what roles do they play in the body?
Proteins are polymers of amino acids that fold into specific 3D shapes. They act as enzymes, structural components, transporters, messengers, and parts of the immune system.
What is an enzyme and how does it work?
An enzyme is a biological catalyst, usually a protein. It binds a substrate at its active site, lowers the activation energy, and speeds up a chemical reaction; activity can be regulated by pH, temperature, cofactors, and inhibitors.
What are the levels of protein structure?
Primary: amino acid sequence; Secondary: alpha helices and beta sheets; Tertiary: overall 3D folding of a single chain; Quaternary: arrangement of multiple chains.
What factors affect enzyme activity?
Temperature, pH, substrate concentration, and the presence of inhibitors or activators; cofactors and coenzymes and denaturation at extreme conditions also influence activity.
What are cofactors and coenzymes?
Cofactors are inorganic ions that assist enzymes; coenzymes are organic molecules (often vitamins) that transfer electrons or groups during reactions.