All the energy in the world come from what source?
The sun! 🌞
Define potential energy and kinetic energy in the simplest way possible:
Potential = energy that can be used
Kinetic = energy that is in motion
How many laws of thermodynamics are there?
Two
What is the first law of thermodynamics?
Energy cannot be created or destroyed, only converted. [during every conversion, some energy is lost as heat]
What is the second law of thermodynamics?
Entropy (the likeliness of randomness) increases.
How do you define free energy?
Free energy is the energy that is available (free) to do work.
ΔG
Change in free energy.
Positive ΔG
Not spontaneous, requires input of energy, products have more free energy than reactants = endergonic.
Negative ΔG
Spontaneous, doesn’t require input of energy, reactants have more free energy than reactants = exergonic.
How would you define activation energy?
Activation energy is the energy required to start up a reaction.
How do you increase the rate activation energy?
Increasing energy by heating up molecules, or simply lowering the energy needed to increase the rate.
What does ATP stand for & what is its structure?
Adenosine Triphosphate = five carbon sugar, adenine, chain of three phosphates.
What’s better for short term energy and what’d better for long term?
Short term = ATP, long term = fats and carbs.
ATP + H2O =
ADP + Pi
The active site of a substrate is where
the enzyme binds.
When an enzyme and a substrate combine, it creates a complex.
This is called an induced fit because it lowers activation energy.
Two factors that can affect how the enzyme works include:
temperature & pH.
Inhibitors are substances that
bind with the enzyme to decrease its activity.
There are two types of inhibitors:
competitive and noncompetitive.
A competitive inhibitor works by?
It works by competing with the substrate to bind to the active site.
A noncompetitive inhibitor works by?
It works by bind to the enzyme to the allosteric site (everything other than the active site), which makes the substrate’s shape change.
Allosteric enzymes
are enzymes that exist in both active and inactive forms.
Allosteric inhibitors
bind to the allosteric site and reduce enzyme activity.
Allosteric activators
bind to the allosteric site and increase the enzyme activity.