AP Biology “What You Need To KNOW” for Free Energy, Thermodynamics, ATP, and Enzymatics Test
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Apply the first and second LAW of thermodynamics to any type of question.
Be able to explain different forms of energy including kinetic, thermal, chemical, usable chemical, free,
potential.
Be able to look at different types of free energy graphs of reactions and explain if the reaction is
exergonic/endergonic, catabolic/anabolic, spontaneous/non-spontaneous.
Be able to explain what energy of activation is and how an enzyme lowers this.
Be able to explain – ΔG vs. + ΔG
Create a model of ATP by drawing shapes that represent the three components of ATP and showing how
they are bonded together to create ATP.
Students should be able to identify , adenosine , AMP , ADP, and ATP
Students should be able to explain why adenine is a base by explaining what happens to hydrogen ions
when adenine is placed in water.
Be able to explain why phosphate is an acid by explaining what happens to hydrogen ions when
phosphate is placed in water.
Be able to explain how ATP provides usable chemical energy by explaining the properties of Triphosphate.
Be able to model and explain how ATP is used to complete tasks “work” in the cell.
Explain a specific chemical, mechanical, and transport mechanism using ATP as an energy coupling
molecule.
Explain energy coupling in detail utilizing ΔG = -7.3 kcal/mol . How much work can it do???
Compare / Contrast induced fit and lock and key dynamics in an enzymatic process.
Be able to look at molecules and explain whether it is polar or non-polar
Be able to explain enzyme / substrate specificity using shape and polarity
Be able to explain how enzymes are regulated by allosteric molecules
Model/explain competitive and non-competitive inhibition
Model/explain how cofactors help enzyme catalyzed reactions
Explain the difference/similarity between minerals and vitamins (coenzymes) and provide 5 examples of
each.
Be able to apply primary, secondary, tertiary, and quaternary structure to the shape and function of an
enzyme.
Be able to explain the 4 different type of amino acid interactions that help form tertiary structure.
Be able to explain in detail how pH and salt concentration affects tertiary structure
Be able to explain and apply knowledge of enzyme kinetics including change in enzyme concentration,
substrate concentration, temperature, and pH.
Be able to model / explain metabolic pathways and explain how they increase metabolic efficiency in a
living cell.
Explain feedback inhibition in detail. Make sure that you explain how this process increases metabolic
efficiency within the cell.
Explain why temperature change is NOT utilized to regulate enzymatic pathways in a living cell.
Be able to explain/model how membrane-bound organelles increase metabolic efficiency in eukaryotic
cells.
Explain why prokaryotic cells have to be small.
Know everything about the polyphenoloxidase lab (isomer portion & inquiry portion)
Be able explain oxidation and reduction in a chemical reaction
Be able to explain why polyphenoloxidase breaks down catechol but not hydroquinone or resorcinol.
Be able to create a graph representing any type of enzymatic reaction and explain the results.
Be able to interpret any type of graph including SEM X 2.
Be able to explain that SEM X 2 is a statistical value that helps us display data with confidence.
Be able to explain how EDTA, Fruit fresh, and salt affects the rate of catechol oxidation.