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Structures, properties, and protein organization levels
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Classify side chains: nonpolar (Gly, Ala, Val, Leu, Ile, Pro, Phe, Met, Trp), polar uncharged (Ser, Thr, Cys, Tyr, Asn, Gln), acidic (Asp, Glu), and basic (Lys, Arg, His). Know the special cases โ glycine is achiral, proline kinks helices, cysteine forms disulfides, and histidine's near 6 makes it the physiological proton shuttle. Chiral amino acids appear as L-isomers in proteins.
At physiological pH, amino acids are zwitterions: carboxylate negative, ammonium positive. A group is protonated when pH is below its . The isoelectric point averages the two values flanking the neutral species: Acidic residues have low pI, basic residues high; charge at a given pH predicts electrophoretic behavior.
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Primary structure is the peptide-bonded sequence; secondary structure (alpha-helices, beta-sheets) is backbone hydrogen bonding; tertiary structure folds via side-chain interactions โ hydrophobic packing, hydrogen bonds, salt bridges, disulfide bonds; quaternary structure assembles multiple subunits (hemoglobin). Denaturation destroys folding but not peptide bonds.