ACS Biochemistry Exam Prep 9 Week Study Plan

Week 1 — Part I: Biochemical Foundations — Water, Thermodynamics, and pH

Difficulty: Moderate–Heavy — High Yield 

What it covers: Water’s polarity, hydrogen bonding, and their consequences for cohesion, high heat capacity, and hydrophobic interactions; thermodynamic quantities (ΔH, ΔS, ΔG, ΔG°′, coupling, spontaneity); standard free energy vs. actual free energy; and quantitative pH topics including pKa, Henderson–Hasselbalch, buffers, titration curves, and biological buffer systems.

Print: 1 Mind Map, 3 Comparison Charts, 3 Cornell Notes pages

Study Tasks

☐ Read the Study Guide first — work through High‑Yield Objectives, Key Terms & Definitions, Concept Overview, and Study Tips before opening the main text.

☐ Highlight as you read — Made Easy Highlighting System

☐ Drill Henderson–Hasselbalch problems until you can: move between pH, pKa, and ratio [A⁻]/[HA]; sketch buffer regions from a titration curve; and explain in words why buffers are most effective within ±1 pH unit of pKa.

☐ Practice conceptual thermodynamics: for each example reaction given, label it as exergonic or endergonic under standard and cellular conditions, and explain how coupling to ATP hydrolysis (or another exergonic step) changes net ΔG.

☐ Complete the Practice Questions for Part I in your quiz bank. Review every rationale — especially for questions involving buffer composition, ΔG vs. ΔG°′, and interpreting sigmoidal titration curves.

How to Use Your Templates

Mind Map:

• Central node = “Water, Thermodynamics, and pH.” Main branches:

• Water’s Properties → polarity, hydrogen bonding, cohesion, high boiling point, hydrophobic effect

• Thermodynamics → ΔH, ΔS, ΔG, ΔG°′, coupling, spontaneity, standard vs. physiological state

• pH & pKa → Henderson–Hasselbalch, titration curves, buffer capacity, biological buffers

• Application Examples → protein folding, acid–base behavior of amino acids, biochemical reaction direction.

Comparison Charts:

• Chart 1 — ΔG vs. ΔG°′ vs. Q: definition, what each “sees” (standard vs. actual), sign interpretation, when a reaction can proceed with positive ΔG°′. 

• Chart 2 — Strong vs. weak acids/bases in biochem: dissociation behavior, buffer usefulness, typical biological examples (e.g., phosphate, bicarbonate, amino acid side chains). 

• Chart 3 — Water vs. nonpolar solvents: dielectric constant, H‑bonding ability, solubility of ions/polar molecules, stabilization of the hydrophobic effect.

Cornell Notes:

• Page 1 — Cue questions: “How does the hydrophobic effect differ from ‘hydrophobic interactions’?” “What does it mean for ΔG to be negative but ΔH positive?” 

• Page 2 — Cue questions: “Write and apply Henderson–Hasselbalch in three different ways (solve for pH, for pKa, for ratio).” “How do you identify the buffer region and equivalence point on a titration curve?” 

• Page 3 — Cue questions: “Why are HEPES, phosphate, and bicarbonate buffers biologically important, and what pH ranges do they cover?”