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MCAT 1A · Bio/Biochem

Amino Acids, Proteins and Enzymes

423 original Anki flashcards, an 11-page illustrated study guide, a 3-page cheat sheet and 53 practice questions for MCAT content category 1A.

What is inside

  • deck.apkg423 original Anki flashcards (233 short answer, 72 multiple choice, 61 cloze, 52 true/false, 5 image occlusion), 23 original diagrams
  • guide.pdf11-page illustrated study guide that explains the ideas
  • cheatsheet.pdf3 printable pages, US Letter at 100 percent
  • questions.pdf53 original MCAT-style practice questions with explanations, including 4 passage-based sets
  • README.txtimport steps
  • 233 short answer
  • 72 multiple choice
  • 61 cloze
  • 52 true/false
  • 5 image occlusion

Topics (40)

  • 01AmAmino acid general structure and alpha carbon
  • 02StStereochemistry of amino acids (L and D, R and S)
  • 03SiSide chain classes: nonpolar, aromatic, polar, acidic, basic
  • 04OnOne- and three-letter codes
  • 05SiSide chain pKa values and charge at physiological pH
  • 06TiTitration curves and isoelectric point
  • 07HeHenderson-Hasselbalch applied to amino acids
  • 08SpSpecial residues: Gly, Pro, Cys, His, Met
  • 09EsEssential versus nonessential amino acids
  • 10PePeptide bond formation, resonance and hydrolysis
  • 11DiDisulfide bonds and cystine
  • 12PrPrimary structure
  • 13SeSecondary structure: alpha helix and beta sheet
  • 14TuTurns, loops, phi and psi angles
  • 15TeTertiary structure and stabilizing forces
  • 16QuQuaternary structure and subunits
  • 17HyHydrophobic effect and protein folding thermodynamics
  • 18ChChaperones, misfolding and prions
  • 19DeDenaturation agents and reversibility
  • 20CoConjugated proteins, prosthetic groups and glycoproteins
  • 21FiFibrous structural proteins: collagen, keratin, elastin
  • 22MoMotor proteins: myosin, kinesin, dynein
  • 23BiBinding proteins, receptors and antibodies
  • 24HeHemoglobin and myoglobin oxygen binding
  • 25EnEnzyme classification (EC classes)
  • 26AcActive site models: lock and key, induced fit
  • 27CaCatalysis mechanisms and transition-state stabilization
  • 28CoCofactors, coenzymes and vitamins
  • 29AcActivation energy and what enzymes do not change
  • 30MiMichaelis-Menten kinetics: Km, Vmax, kcat
  • 31CaCatalytic efficiency (kcat/Km) and reaction order
  • 32LiLineweaver-Burk plots
  • 33CoCompetitive inhibition
  • 34NoNoncompetitive and mixed inhibition
  • 35UnUncompetitive inhibition
  • 36IrIrreversible inhibition and suicide substrates
  • 37AlAllosteric regulation and cooperativity (Hill coefficient)
  • 38CoCovalent modification, zymogens and feedback inhibition
  • 39EfEffects of temperature and pH on enzymes
  • 40PrProtein isolation and analysis: electrophoresis, chromatography, assays

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  4. Print the PDFs on US Letter at 100 percent, or read them on screen.

Previews

Look before you buy.

Sample card (answer side)
Sample card (answer side)
Sample card (answer side)
Sample card (answer side)
Cheat sheet, page 1 (partial preview)
Cheat sheet, page 2 (partial preview)
Study guide, page 1 (partial preview)
Study guide, page 2 (partial preview)

Try it · sample practice questions

Five questions from the pack.

0 of 5 answered

Q1What is the approximate net charge of the tripeptide Lys-Asp-Gly at pH 7.4?

B. At pH 7.4 the free N-terminal amine is +1, the Lys side chain is +1, the Asp side chain is -1, and the free C-terminal carboxylate is -1, for a net charge of 0. Answering +1 or +2 forgets one or both negative groups, and -1 forgets the N-terminus.

Q2Why does the peptide bond not rotate freely?

D. Delocalization of the nitrogen lone pair onto oxygen makes the amide plane rigid. A hydrogen bond, ionic bond, or disulfide would be a different type of interaction and would not describe the amide linkage.

Q3An enzyme transfers an amino group from one molecule to another. Which EC class?

A. Group transfer defines EC 2 (transferases), as with aminotransferases. Ligases join molecules using ATP, lyases cleave without water or redox, and isomerases rearrange one molecule.

Q4Aspirin inhibits cyclooxygenase by:

A. Aspirin transfers an acetyl group to a Ser, permanently blocking the enzyme. Reversible competitors (such as ibuprofen) behave differently, and aspirin does not target ES or heme.

Q5Iron in the heme of hemoglobin must be in which state to bind oxygen?

A. Fe2+ (ferrous) binds O2 reversibly. Fe3+ (methemoglobin) does not bind oxygen, and Fe0 and Fe4+ are not the physiological states in heme.

Those are real questions from the pack, word for word.

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