DAT Advanced: Metabolism, Kinetics & PAT Mastery
Advanced DAT preparation covering cellular respiration, enzyme kinetics, thermochemistry, spectroscopy, and advanced perceptual ability techniques for competitive scores.
Master advanced DAT concepts with free flashcards and targeted practice strategies. This lesson builds on foundational knowledge to tackle cellular respiration pathways, enzyme kinetics and inhibition, thermochemistry and equilibrium, spectroscopy and molecular structure analysis, plus advanced perceptual ability test techniquesβessential topics for achieving competitive DAT scores in the 90-minute science sections and PAT.
Welcome to Lesson 3: Advanced DAT Content π§¬π¬
You've mastered the fundamentals and intermediate conceptsβnow it's time to elevate your performance with the complex, interconnected topics that separate good scores from great ones. This lesson focuses on high-yield advanced material that appears repeatedly on the DAT:
- Biology: Cellular respiration (glycolysis β Krebs cycle β ETC), enzyme kinetics (Michaelis-Menten, competitive/non-competitive inhibition)
- General Chemistry: Thermochemistry (Hess's Law, bond energy), chemical equilibrium (Le Chatelier's principle, Ksp), spectroscopy fundamentals
- Organic Chemistry: Spectroscopy (IR, NMR, mass spec), advanced reaction mechanisms, synthesis pathways
- Perceptual Ability: Advanced strategies for cube counting, pattern folding, and view recognition
These topics require integration of multiple conceptsβexactly what the DAT tests at higher difficulty levels.
π‘ Test Strategy Tip: The DAT science sections aren't just about knowing factsβthey test your ability to apply concepts under time pressure. Aim for 75-80 seconds per question, flagging anything over 90 seconds for review.
𧬠Biology: Cellular Respiration Deep Dive
The ATP Production Pathway
Cellular respiration is the highest-yield metabolism topic on the DAT. You must know:
- Where each stage occurs
- What goes in and comes out
- How much ATP is produced
- Regulation points (rate-limiting steps)
π Cellular Respiration Quick Reference
| Stage | Location | Input | Output | ATP Yield |
|---|---|---|---|---|
| Glycolysis | Cytoplasm | 1 Glucose | 2 Pyruvate, 2 NADH | 2 ATP (net) |
| Pyruvate Oxidation | Mitochondrial matrix | 2 Pyruvate | 2 Acetyl-CoA, 2 NADH, 2 COβ | 0 ATP |
| Krebs Cycle | Mitochondrial matrix | 2 Acetyl-CoA | 4 COβ, 6 NADH, 2 FADHβ | 2 ATP |
| ETC + Oxidative Phosphorylation | Inner mitochondrial membrane | 10 NADH, 2 FADHβ | HβO | ~28 ATP |
| TOTAL | ~32 ATP | |||
π§ Mnemonic for Glycolysis Steps: "Goodness Gracious, Father Franklin Did Go By Picking Pumpkins Patiently Every Pumpkin"
- Glucose β Glucose-6-P β Fructose-6-P β Fructose-1,6-BP β DHAP/G3P β 1,3-BPG β 3-PG β 2-PG β PEP β Pyruvate
Key Regulatory Points (memorize these!):
- Glycolysis: Phosphofructokinase (PFK) - inhibited by ATP/citrate, activated by AMP/ADP
- Krebs Cycle: Isocitrate dehydrogenase - inhibited by ATP/NADH, activated by ADP/CaΒ²βΊ
- ETC: Complex IV (cytochrome oxidase) - inhibited by cyanide
CELLULAR RESPIRATION OVERVIEW
CYTOPLASM MITOCHONDRION
ββββββββββββββββββββ βββββββββββββββββββββββββββ
β β β Matrix β IMS β
β GLUCOSE β β β β
β β β β Pyruvate β β
β Glycolysis ββββββΌβββββ β β β
β β β β Acetyl-CoA β β
β 2 Pyruvate β β β β β
β 2 ATP β β Krebs Cycle β β
β 2 NADH β β β β Inner β
β β β NADH, FADHβ βββΌβββ ETC β
β β β β β β
β β β β ATP β
ββββββββββββββββββββ βββββββββββββββββββββββββββ
HβΊ gradient
π‘ DAT Tip: Questions often ask about oxygen deprivation. Without Oβ, the ETC stops β NADH can't be recycled β Krebs cycle stops β only glycolysis continues (producing lactate). Net ATP: just 2!
Enzyme Kinetics: Michaelis-Menten & Inhibition
Enzyme questions appear in both biology and general chemistry sections. Master these concepts:
Michaelis-Menten Equation: v = (Vmax Γ [S]) / (Km + [S])
- Vmax: Maximum reaction velocity (when enzyme is saturated)
- Km: Substrate concentration at Β½ Vmax (indicates enzyme affinityβlower Km = higher affinity)
- Kcat: Turnover number (reactions per enzyme per second)
| Inhibitor Type | Binding Site | Effect on Vmax | Effect on Km | Overcome by [S]? |
|---|---|---|---|---|
| Competitive | Active site | Unchanged | Increases | Yes |
| Non-competitive | Allosteric site | Decreases | Unchanged | No |
| Uncompetitive | ES complex only | Decreases | Decreases | No |
π§ Memory Device: "Competitive = Can be Conquered by substrate" (increasing [S] overcomes competitive inhibition)
Lineweaver-Burk Plot (double reciprocal plot): 1/v vs 1/[S]
- Y-intercept = 1/Vmax
- X-intercept = -1/Km
- Slope = Km/Vmax
β οΈ Common Mistake: Students confuse competitive and non-competitive. Remember: if the inhibitor competes for the active site, you can overcome it by adding more substrate!
π§ͺ General Chemistry: Thermochemistry & Equilibrium
Hess's Law and Bond Energy Calculations
Hess's Law: Total enthalpy change is independent of pathwayβonly depends on initial and final states.
ΞHΒ°rxn = Ξ£ ΞHΒ°f(products) - Ξ£ ΞHΒ°f(reactants)
Alternative using bond energies: ΞHΒ°rxn = Ξ£(Bonds broken) - Ξ£(Bonds formed)
π‘ Key Insight: Breaking bonds requires energy (endothermic, positive), forming bonds releases energy (exothermic, negative)
π§ Practice Scenario: Calculate ΞH for: CHβ + 2Oβ β COβ + 2HβO
Given bond energies:
- C-H: 413 kJ/mol
- O=O: 498 kJ/mol
- C=O: 799 kJ/mol
- O-H: 463 kJ/mol
| Step | Calculation | Result |
|---|---|---|
| 1. Bonds broken | 4(C-H) + 2(O=O) = 4(413) + 2(498) | +2648 kJ |
| 2. Bonds formed | 2(C=O) + 4(O-H) = 2(799) + 4(463) | -3450 kJ |
| 3. Net ΞH | 2648 - 3450 | -802 kJ (exothermic) |
Chemical Equilibrium and Le Chatelier's Principle
Equilibrium Constant: K = [products] / [reactants]
- K >> 1: Products favored
- K << 1: Reactants favored
- K β 1: Significant amounts of both
Le Chatelier's Principle: System shifts to counteract stress
LE CHATELIER STRESS RESPONSES
STRESS SHIFT DIRECTION
ββββββββββββββ βββββββββββββββββββ
Add reactant β Forward (β)
Add product β Reverse (β)
Increase T β Endothermic direction
Decrease T β Exothermic direction
Increase P β Fewer moles of gas
Add catalyst β NO SHIFT (faster equilibrium)
β οΈ Common Mistake: Catalysts don't shift equilibriumβthey just help reach it faster! K remains unchanged.
Solubility Product (Ksp): For precipitation reactions
For AgCl(s) β AgβΊ(aq) + Clβ»(aq): Ksp = [AgβΊ][Clβ»]
- If Q < Ksp: No precipitate (unsaturated)
- If Q = Ksp: Saturated solution
- If Q > Ksp: Precipitation occurs
π§ Mnemonic: "Questionable β Query if solid forms" (compare Q to Ksp)
Spectroscopy Fundamentals for General Chemistry
Beer-Lambert Law: A = Ξ΅bc
- A = absorbance (no units)
- Ξ΅ = molar absorptivity (LΒ·molβ»ΒΉΒ·cmβ»ΒΉ)
- b = path length (cm)
- c = concentration (mol/L)
π‘ DAT Application: If absorbance doubles, concentration doubles (direct relationship)
Electromagnetic Spectrum Energy:
E = hΞ½ = hc/Ξ»
- Higher frequency β Higher energy
- Shorter wavelength β Higher energy
Order (increasing energy): Radio < Microwave < Infrared < Visible < Ultraviolet < X-ray < Gamma
π§ Mnemonic: "Rabbits Munch Icy Veggies Under Xotic Gardens"
βοΈ Organic Chemistry: Spectroscopy & Reaction Integration
IR Spectroscopy: Functional Group Identification
Key absorption ranges (memorize these wavenumbers!):
| Functional Group | Wavenumber (cmβ»ΒΉ) | Appearance | Memory Tip |
|---|---|---|---|
| O-H (alcohol) | 3200-3600 | Broad | "OH so broad!" |
| O-H (carboxylic acid) | 2500-3300 | Very broad | Even broader than alcohol |
| N-H | 3300-3500 | Sharp (2 peaks if primary) | "N" for narrow |
| C=O (carbonyl) | 1650-1750 | Strong, sharp | "King of the spectrum" |
| C=C | 1620-1680 | Medium | Just below C=O |
| C-H (alkane) | 2850-3000 | Medium | "Alkanes are plain" |
| Cβ‘C | 2100-2260 | Medium, sharp | Triple bonds = middle range |
| Cβ‘N | 2210-2260 | Medium | Similar to Cβ‘C |
π§ Master Mnemonic for Carbonyl Region: "AAEK" (decreasing wavenumber)
- Acid chloride: ~1800 cmβ»ΒΉ
- Aldehyde: ~1730 cmβ»ΒΉ
- Ester: ~1735 cmβ»ΒΉ
- Ketone: ~1715 cmβ»ΒΉ
ΒΉH NMR Spectroscopy: Chemical Shift & Splitting
Chemical Shift (Ξ΄) Ranges (ppm from TMS):
NMR CHEMICAL SHIFT REGIONS
12-10 10-9 9-7 7-4 4-1 1-0 Ξ΄ (ppm)
β β β β β β
β β β β β β
COOH CHO Aromatic O-CH N-CH Alkyl
Acid Aldehyde H's Alcohol Amine R-CHβ
Ether
Splitting Patterns (n+1 rule):
- n = number of equivalent neighboring H's
- Pattern: n+1 peaks
| Neighbors | Pattern | Ratio |
|---|---|---|
| 0 | Singlet | 1 |
| 1 | Doublet | 1:1 |
| 2 | Triplet | 1:2:1 |
| 3 | Quartet | 1:3:3:1 |
| 4 | Quintet | 1:4:6:4:1 |
π‘ Integration: Area under peak = number of H's (relative)
Mass Spectrometry: Molecular Ion & Fragmentation
M peak (molecular ion): Tells molecular weight
M+1 peak: Indicates number of carbons (1.1% per C due to ΒΉΒ³C)
Common fragment losses:
- -15: Loss of CHβ (methyl)
- -18: Loss of HβO (dehydration from alcohol)
- -28: Loss of CO (from aldehydes/ketones) or CHβ=CHβ
- -29: Loss of CHO (from aldehydes)
- -45: Loss of COβH (from carboxylic acids)
π§ Practice: M peak at 88, strong peak at 73. What was lost?
- 88 - 73 = 15 β Lost CHβ group!
Synthesis Pathway Strategy
DAT synthesis questions test your ability to work backwards from product:
SYNTHESIS PROBLEM APPROACH
1. Identify functional groups in PRODUCT
β
2. What reactions CREATE those groups?
β
3. Identify functional groups in STARTING MATERIAL
β
4. What reactions convert starting β intermediate?
β
5. Chain reactions together
β
6. Check for unwanted side reactions
Key Transformations (memorize these!):
| Starting FG | Reagent | Product FG |
|---|---|---|
| Alkene | 1. BHβ/THF 2. HβOβ, OHβ» | Alcohol (anti-Markovnikov) |
| Alkene | HβO, HβSOβ | Alcohol (Markovnikov) |
| Alcohol (1Β°) | PCC or DMP | Aldehyde |
| Alcohol (1Β°) | CrOβ, HβSOβ | Carboxylic acid |
| Alcohol (2Β°) | PCC, CrOβ, etc. | Ketone |
| Alkyne | 1. Oβ 2. HβO | Carboxylic acids |
| Benzene | Brβ, FeBrβ | Bromobenzene |
β οΈ Common Mistake: Forgetting oxidation limits! Primary alcohols can be oxidized to aldehydes (mild) OR carboxylic acids (strong). Secondary alcohols only go to ketones. Tertiary alcohols don't oxidize!
πΊ Perceptual Ability Test: Advanced Strategies
Cube Counting: Systematic Approach
Cube counting appears deceptively simple but requires systematic analysis:
The Layer Method:
- Count cubes by number of exposed sides (painted faces)
- Work layer by layer (top β bottom)
- Account for internal cubes (0 painted sides)
CUBE COUNTING STRATEGY
Top View of 3Γ3Γ3 cube:
βββ¬ββ¬ββ
βββββββ β = 3 sides exposed (corner)
βββΌββΌββ€ β = 2 sides exposed (edge)
βββββββ Β· = 1 side exposed (face)
βββΌββΌββ€ β‘ = 0 sides exposed (internal)
βββββββ
βββ΄ββ΄ββ
3Γ3Γ3 Analysis:
- 3 exposed sides: 8 cubes (corners)
- 2 exposed sides: 12 cubes (edges)
- 1 exposed side: 6 cubes (faces)
- 0 exposed sides: 1 cube (center)
Total: 27 cubes
π‘ Time-Saving Trick: For standard stacks, memorize common configurations:
- 2Γ2Γ2 = 8 cubes (all corners, 0 with 0 sides, 0 with 1 side)
- 3Γ3Γ3 = 27 cubes (8 corners, 12 edges, 6 faces, 1 center)
- 4Γ4Γ4 = 64 cubes (8 corners, 24 edges, 24 faces, 8 internal)
Pattern Folding: The Corner Method
Strategy: Focus on corner configurations and adjacent face relationships
When a pattern folds:
- Identify the base (usually bottom/center)
- Track which edges connect (become adjacent when folded)
- Check corner meetings (3 faces meet at each corner)
- Verify pattern orientation (rotation/flipping)
PATTERN FOLDING EXAMPLE
Flat pattern: Folded cube:
[A] [D]
[B][C][D] [B] C [A]
[E] [E]
Corner analysis:
- Top-front-right corner: A, C, D meet
- Check orientations match answer choices
π§ Practice Tip: Use your knuckles! Each knuckle joint represents a face. Move your finger to simulate folding.
View Recognition: Orthogonal Projection Rules
Key Principles:
- Top view: Shows outlines, highest points visible
- Front view: Shows height, front-most surfaces
- Side view: Shows depth, side profiles
- Each view is a 2D projection of 3D object
VIEW RECOGNITION STRATEGY
3D Object Analysis:
TOP VIEW
βΌ
βββββββββββ
β β
βββββ€ OBJ βββββ SIDE VIEW
β β
βββββββββββ
β²
FRONT VIEW
Check each view:
β Heights match
β Widths align
β Depths consistent
β Look for contradictions
π‘ Elimination Strategy: Often 3-4 answer choices can be quickly eliminated by finding one contradictory feature in any single view.
Angle Ranking: Reference Angle Technique
The 45Β° Benchmark Method:
- 45Β° is your reference (mentally divide right angle in half)
- Compare each angle to 45Β°
- Rank as: much less, slightly less, about 45Β°, slightly more, much more
ANGLE ESTIMATION GUIDE
90Β°β 60Β°β 45Β°β 30Β°β
β / / /
β / / /
β / / /
βββββββ΄ββββ/ββββββ/ββββββ/ββββββββ
Right Obtuse Ref Acute
β‘ Speed Tip: Don't measure precisely! Rough estimation + elimination is faster than careful analysis.
Time Management for PAT
Recommended pacing (90 total minutes for PAT section):
| Subtest | Questions | Time Allocation | Seconds/Question |
|---|---|---|---|
| Angle Ranking | 15 | 10 minutes | 40s |
| Hole Punching | 15 | 12 minutes | 48s |
| Cube Counting | 15 | 13 minutes | 52s |
| Pattern Folding | 15 | 18 minutes | 72s |
| View Recognition | 15 | 15 minutes | 60s |
| Buffer/Review | - | 22 minutes | - |
π― Strategy: Cube counting and angle ranking are typically fastestβbuild time buffer here for harder pattern folding questions.
β οΈ Common Mistakes to Avoid
Biology Errors
β Confusing ATP yields: NADH = ~2.5 ATP, FADHβ = ~1.5 ATP (not 3 and 2!)
β
Use the updated, more accurate values
β Forgetting substrate-level vs oxidative phosphorylation: Only 4 ATP come from substrate-level
β
Glycolysis (2) + Krebs (2) = 4 substrate-level; rest is ETC
β Mixing up enzyme inhibition types
β
Draw Lineweaver-Burk plots to visualize differences
Chemistry Errors
β Wrong sign in Hess's Law: ΞHΒ°f values already have correct signs
β
Products minus reactants (don't flip signs!)
β Thinking catalysts shift equilibrium
β
Catalysts speed up forward AND reverse equally
β Forgetting units in Beer-Lambert Law
β
Check that Ξ΅ units match (usually LΒ·molβ»ΒΉΒ·cmβ»ΒΉ)
Organic Chemistry Errors
β Confusing IR peaks: O-H vs N-H both appear ~3300-3500 cmβ»ΒΉ
β
O-H is broader; N-H shows 2 sharp peaks if primary amine
β Ignoring NMR integration
β
Integration tells you relative H countβcritical for structure determination
β Forgetting oxidation limitations
β
3Β° alcohols can't be oxidized (no H on carbon bearing OH)
PAT Errors
β Not being systematic in cube counting (missing internal cubes)
β
Use layer method every time
β Getting disoriented in pattern folding
β
Mark the base face, track adjacent relationships
β Spending too long on one difficult question
β
Flag and move on after 90 seconds
π‘ Key Takeaways
π― Master These High-Yield Concepts
Biology
- Cellular respiration: Know location, inputs/outputs, ATP yield for each stage
- Enzyme kinetics: Competitive inhibition (Kmβ, Vmax same), non-competitive (Vmaxβ, Km same)
- Regulation: PFK for glycolysis, isocitrate dehydrogenase for Krebs
General Chemistry
- Hess's Law: ΞH = Ξ£products - Ξ£reactants (or bonds broken - bonds formed)
- Le Chatelier: System opposes stress; catalysts don't shift equilibrium
- Beer-Lambert: A = Ξ΅bc (absorbance proportional to concentration)
Organic Chemistry
- IR: O-H broad (3200-3600), C=O sharp (1650-1750)
- NMR: Aldehyde H (9-10 ppm), aromatic H (7-8 ppm), integration = relative H count
- Mass spec: M peak = molecular weight, common losses (15=CHβ, 18=HβO)
PAT
- Cube counting: Use layer method (cornersβedgesβfacesβinternal)
- Pattern folding: Focus on corners (3 faces meet)
- View recognition: Eliminate by finding contradictions
- Time management: Build buffer on faster sections
π§ Study Strategy: These advanced topics require active practice, not passive review. Do 20-30 practice problems daily, focusing on why answers are correct/incorrect.
β‘ Test Day: In the science sections, if a question requires >90 seconds of calculation, flag it and return later. On PAT, trust your systematic approachβdon't second-guess!
π Further Study
Comprehensive DAT Biology: https://www.khanacademy.org/science/biology
Enzyme Kinetics Deep Dive: https://www.ncbi.nlm.nih.gov/books/NBK22430/
DAT PAT Practice: https://datbootcamp.com/dat-perceptual-ability-test-pat/
π Next Steps
You've now covered advanced DAT content that separates competitive scores from average ones. Practice integration: most difficult DAT questions combine multiple concepts (e.g., enzyme kinetics + thermodynamics, spectroscopy + synthesis). In Lesson 4, we'll tackle DAT "killer questions"βmulti-step problems that require synthesizing knowledge across all sections. Keep drilling these fundamentals! π