Enzyme Kinetics (Activation Energy and Gibb's Free Energy)

The video tutorial covers the kinetics and thermodynamics of enzyme reactions, focusing on the concepts of activation energy, free energy changes, and the role of enzymes. It explains how activation energy affects reaction rates and how enzymes lower this energy to speed up reactions. The tutorial also distinguishes between kinetic and thermodynamic favorability, emphasizing that these are independent concepts. Additionally, it clarifies the difference between exergonic and endergonic reactions and the implications of Delta G values on reaction spontaneity.

What is the relationship between the activation energy and the rate of a reaction?

What is the definition of activation energy in the context of chemical reactions?

Explain the significance of the transition state in a chemical reaction.

What role do intermediates play in a reaction mechanism?

How do enzymes affect the activation energy of a reaction?

Describe how the free energy diagram can be used to determine the spontaneity of a reaction.

What does a negative Delta G value indicate about a reaction?

How can you determine if a reaction is thermodynamically favorable?

Differentiate between exergonic and endergonic reactions.

What is the importance of understanding the difference between kinetics and thermodynamics in biochemical reactions?