Bio exam 3 lesson 1

Kinetic Energy: Energy of motion (e.g., flowing water).
Potential Energy: Stored energy due to structure or location (e.g., water behind a dam, energy in chemical bonds).

Study of Energy Transformations: Governed by two laws.
- First Law: Energy conservation - total energy in the universe is constant, can be transferred/transformed but never created or destroyed.
- Second Law: Entropy increases - every energy transformation increases entropy, reducing energy available for useful work.

Positive ΔG: Non-spontaneous (endergonic) reaction; requires energy. NEEDS ENERGY
Negative ΔG: Spontaneous (exergonic) reaction; releases energy. HAS ENERGY
ΔG indicates free energy available for work in a cell.
- ΔG < 0: Reaction gives off energy.
- ΔG > 0: Reaction requires energy to proceed.
- Each reaction has a specific ΔG which never changes!
- Delta G NEVER changes

Energy must be added for reactions to proceed, exemplified by sunburn converting solar energy to heat energy.

Second Law of Thermodynamics: Energy changes lead to increased entropy (disorder).
Endergonic Reactions: Require energy input to occur; products have more energy than reactants.
Exergonic Reactions: Release energy spontaneously; products have less energy than reactants.
Energy coupling: Endergonic reactions often coupled with exergonic reactions for cellular efficiency.

ATP (Adenosine Triphosphate): Major energy carrier in cells.
Hydrolysis is when you add water to break stuff down
Hydrolysis of ATP releases energy (e.g., $-7.3$ energy units) by breaking a high-energy bond between phosphates.
Converted to ADP (Adenosine Diphosphate) after energy release; can be re-generated in cells.

Delta G: Represents free energy available to do work.
Negative $ext{Delta G}$ indicates energy release (spontaneous reaction); positive indicates energy requirement.
Enzymes do not change $ext{Delta G}$ , but lower activation energy required for reactions.

Enzymes are mostly proteins with specific active sites for catalyzing reactions.
Activation Energy: Minimum energy to start a reaction; enzymes lower this energy barrier.
Enzymes are specific; bind with substrates to form products without altering themselves.
Rates of enzyme reactions vary significantly based on conditions.
Active site is a small pocket in an enzyme where molecules bind and undergo chemical reactions
The substrate is the molecule that goes into the active site to from the chemical reaction. The efficiency of an enzyme can be influenced by factors such as temperature, pH, and substrate concentration. Additionally, the presence of inhibitors can decrease enzyme activity by blocking the active site or altering its shape, thereby preventing the substrate from binding.

Lactose intolerance occurs due to lack of lactose enzyme; affects ability to digest milk products.
Enzyme function can be based on genetic background and environmental factors.

Competitive Inhibition: Blocker competes with substrate for active site.
Noncompetitive Inhibition: Blocker binds elsewhere, altering the enzyme's shape and activity.
Feedback inhibition: Product of a reaction inhibits enzyme activity to maintain balance and conserve resources.

Enzyme reactions can be affected by temperature, pH, and ionic balance, leading to enzyme denaturation if extremes are reached.
Advancements in enzyme applications from extremophiles (heat-loving organisms) utilized in technology.
Turn over # means speed that ab eznyme works