Memly's MCAT Biology and Biochemistry: 350 Key Terms

350 terms, with the biochemistry weighted heaviest.

350 cardsLast updated 2026-08-21

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Knowing a definition is rarely what a passage asks for. It asks what the definition predicts: what happens to apparent Km when the inhibitor binds the enzyme-substrate complex, why a curve shifts right when tissue turns acidic, why a protein stops migrating at one point in a pH gradient, what a band at the wrong size means. Every one of those is a definition plus one more step, and that second step is where the marks are. So every card here gives the definition and then the step that makes it usable, on 313 of the 350. The weighting follows where that reasoning is hardest rather than where content is easiest to list: 44 cards on amino acids and protein structure, 35 on enzymes and kinetics, 95 across bioenergetics and metabolism, 40 on the laboratory methods that generate the data in a passage, 50 on organ system physiology, and the rest across nucleic acids, genetics, carbohydrates and lipids. Cell structure and the step-by-step pathways of respiration and photosynthesis sit in the Cell Biology Essentials deck, so the two fit together rather than repeating each other. Cards are tagged by area and by sub-area, so you can run just enzyme kinetics, just the separation techniques, or just nitrogen metabolism on its own. Import it and the deck joins your spaced-repetition schedule. What you should end up with is the thing a passage actually tests: given a graph, a gel, or a curve, being able to say what it means and what would change it.

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What's inside

Showing 100 representative cards from the full 350-card deck.

Front	Back
Amino acid classification by side chain — what is it?	The twenty standard amino acids sorted by what their side chain does in water, into nonpolar, polar uncharged, acidic, and basic groups. Nearly every question about folding, charge, or a mutation's effect is answered by which group the residue belongs to.
Polar uncharged amino acids — what is it?	Serine, threonine, cysteine, tyrosine, asparagine, and glutamine, whose side chains hydrogen bond without carrying a net charge at neutral pH. Serine, threonine, and tyrosine carry the hydroxyls that kinases phosphorylate, which is why regulation clusters on this group.
Basic amino acids — what is it?	Lysine, arginine, and histidine, whose side chains can accept a proton and carry positive charge. Lysine and arginine are protonated at physiological pH and bind the phosphate backbone of nucleic acids, which is why histones are rich in both.
Aromatic amino acids — what is it?	Phenylalanine, tyrosine, and tryptophan, each carrying a ring in the side chain. They absorb ultraviolet light near 280 nanometres, which is how protein concentration is estimated spectrophotometrically, with tryptophan contributing most.
Cysteine and disulfide bonds — what is it?	A sulfhydryl-bearing residue, two of which can be oxidized to form a covalent disulfide bridge. It is the only covalent cross-link in tertiary and quaternary structure, and it forms in oxidizing environments, which is why disulfides are common in secreted proteins and rare in the cytosol.
Isoelectric point — what is it?	The pH at which a molecule carries no net charge. A protein does not migrate in an electric field at this pH, which is the whole basis of isoelectric focusing, and it is least soluble there because charge repulsion between molecules disappears.
Titration curve of an amino acid — what is it?	A plot of pH against added base showing a plateau at each pKa and a steep rise between them. Buffering capacity is greatest at each pKa, where the species is half deprotonated, and the isoelectric point sits on the steep segment between two plateaus.
Essential amino acids — what is it?	The amino acids an adult human cannot synthesize and must obtain from the diet. The distinction is about biosynthetic capacity rather than importance, and some are conditionally essential when synthesis cannot keep pace with demand.
Peptide bond geometry — what is it?	The amide linkage between residues, which has partial double bond character from resonance and is therefore planar. Free rotation. The bond is rigid and almost always in the trans arrangement.
Alpha helix — what is it?	A right-handed coil held by hydrogen bonds between the backbone carbonyl of one residue and the amide hydrogen four residues along. Side chain bonding. Secondary structure is a backbone phenomenon.
Beta turn — what is it?	A short backbone reversal, typically of four residues, that lets a chain fold back on itself. Glycine and proline dominate turns, the first for flexibility and the second for its built-in kink.
Chaperonin — what is it?	A barrel-shaped complex that encloses a partly folded polypeptide and gives it an isolated chamber in which to fold. Isolation prevents aggregation with neighbouring unfolded chains, which is the main risk in a crowded cytosol.
Protein glycosylation — what is it?	Attachment of carbohydrate to a protein, N-linked through asparagine or O-linked through serine or threonine. The sugar governs folding quality control, stability, and cell surface recognition.
Hemoglobin quaternary structure — what is it?	A tetramer of two alpha and two beta subunits, each holding a haem group with a central iron. Having four subunits is what makes cooperative binding possible, since one subunit can report its state to the others.
2,3-bisphosphoglycerate — what is it?	A glycolytic side product that binds in the central cavity of deoxyhemoglobin and stabilizes the low-affinity state. Its concentration rises at altitude and in chronic hypoxia, which shifts the curve right and improves unloading without changing hemoglobin itself.
Oxidoreductases — what is it?	Enzymes catalyzing electron transfer, usually paired with a nicotinamide or flavin coenzyme.
Lyases — what is it?	Enzymes breaking a bond without water and without oxidation, often leaving a double bond, or adding a group across one. Ligases, which join molecules and require energy input.
Transition state stabilization — what is it?	The central catalytic strategy, in which the active site binds the transition state more tightly than the substrate. Lowering the energy of the highest point on the path is what reduces activation energy, so a molecule resembling the transition state is a very tight inhibitor.
Serine protease catalytic triad — what is it?	Serine, histidine, and aspartate arranged so that histidine deprotonates serine and aspartate orients histidine. The three residues are distant in sequence and adjacent in the folded protein, which is a standard illustration that function follows tertiary structure.
Michaelis-Menten equation — what is it?	The relationship giving initial reaction velocity as a function of substrate concentration, rising hyperbolically to a maximum.
Lineweaver-Burk plot — what is it?	A double reciprocal plot of one over velocity against one over substrate concentration, giving a straight line. Inhibition types are told apart by which intercept moves, which is much harder to see on the hyperbolic plot.
Uncompetitive inhibition — what is it?	An inhibitor that binds only the enzyme-substrate complex, lowering both Km and Vmax. Removing the complex pulls the binding equilibrium forward, which is why apparent affinity appears to improve while output falls.
Sigmoidal kinetics of an allosteric enzyme — what is it?	A velocity curve that is S-shaped rather than hyperbolic, so Michaelis-Menten analysis does not describe it. The shape comes from cooperativity between subunits, which makes the enzyme act as a switch across a narrow substrate range.
Isozymes — what is it?	Distinct proteins catalyzing the same reaction with different kinetic properties, often expressed in different tissues.
Coenzyme A — what is it?	A pantothenate-derived carrier that binds acyl groups through a high-energy thioester bond. The thioester is what makes an acyl group transferable, so coenzyme A appears wherever two-carbon and larger acyl units move between pathways.
Aldose and ketose — what is it?	Sugars classified by whether the carbonyl sits at the end of the chain as an aldehyde or within it as a ketone. Only the aldehyde form is directly oxidizable, which is why ketoses must isomerize before they register in a reducing sugar test.
Mutarotation — what is it?	The spontaneous interconversion of alpha and beta anomers in solution, passing through the open chain form. A pure anomer dissolved in water relaxes to an equilibrium mixture, which is why optical rotation drifts to a fixed value.
Reducing sugar — what is it?	A sugar with a free anomeric carbon, able to open to the aldehyde and be oxidized. Sucrose is not reducing because both anomeric carbons are locked in its glycosidic bond, while lactose and maltose are.
D and L designation in sugars — what is it?	Assignment made from the chiral carbon furthest from the carbonyl, with the hydroxyl on the right in a Fischer projection defining D. Essentially all biological sugars are D, which is the mirror image of the convention for amino acids, where the L form predominates.
Fatty acid nomenclature — what is it?	A fatty acid is described by chain length and by the number and position of double bonds. Position is counted from the carboxyl carbon in systematic naming and from the methyl end in omega naming, so the same molecule carries two different numbers.
Why fat stores more energy than carbohydrate — can you explain it?	Fatty acid carbons are more reduced than sugar carbons and triacylglycerols are stored without water. The energy difference is roughly twofold per gram before hydration is counted, and considerably more once it is, which is why long-term storage is lipid rather than glycogen.
Steroid backbone — what is it?	Four fused rings, three of six carbons and one of five. Members differ only in attached functional groups and oxidation state, which is why testosterone and estradiol are close relatives despite opposite effects.
Micelle, bilayer and liposome — what is it?	A micelle is a single-tailed aggregate with a hydrophobic core, a bilayer is a two-leaflet sheet, and a liposome is a closed bilayer vesicle with an aqueous interior. Which one forms depends on the shape of the molecule, so single-tailed detergents make micelles and two-tailed phospholipids make bilayers.
Nucleoside and nucleotide — what is it?	A nucleoside is a base joined to a sugar. A nucleotide adds one or more phosphates. Polymerases add nucleoside triphosphates and release pyrophosphate, so the triphosphate supplies both the residue and the energy for the bond.
DNA melting temperature — what is it?	The temperature at which half of a DNA population has separated into single strands.
DNA supercoiling — what is it?	Over- or under-winding of the double helix relative to its relaxed state. Unwinding at a replication fork drives positive supercoils ahead of it, which would stall the fork if they were not relieved.
Proofreading by DNA polymerase — what is it?	A 3' to 5' exonuclease activity that excises a mismatched nucleotide immediately after it is added. It acts during synthesis, which distinguishes it from repair systems that act afterward, and it accounts for most of replication's accuracy.
Eukaryotic RNA polymerases — what is it?	Polymerase I makes most ribosomal RNA, polymerase II makes messenger RNA and several small RNAs, and polymerase III makes transfer RNA and one ribosomal RNA. Only the polymerase II transcripts are capped and polyadenylated, so processing follows from which enzyme made the transcript.
Polycistronic messenger RNA — what is it?	A single transcript encoding several proteins, each with its own start and stop signals. It is a prokaryotic arrangement that follows from operon organization, and eukaryotic transcripts are monocistronic instead.
Ribosomal A, P and E sites — what is it?	The A site accepts the incoming charged transfer RNA, the P site holds the growing chain, and the E site releases the deacylated transfer RNA. The order A to P to E is the direction of movement during translocation, so naming the site names the stage.
Nonsense-mediated decay — what is it?	A surveillance pathway degrading transcripts carrying a premature stop codon. It prevents accumulation of truncated proteins, so a nonsense mutation often removes the message rather than producing a short protein.
High-energy phosphate compounds — what is it?	Molecules whose phosphate transfer releases a large amount of free energy, including ATP, creatine phosphate, phosphoenolpyruvate, and 1,3-bisphosphoglycerate. The energy is in the difference between reactant and product stability, from charge repulsion and resonance in the released phosphate, not in the bond itself.
Redox potential and electron flow — what is it?	A measure of a species' tendency to accept electrons, with electrons flowing spontaneously toward the more positive potential. The respiratory chain is ordered by increasing potential, ending at oxygen, so the sequence of carriers is set by thermodynamics rather than by convention.
Investment and payoff phases of glycolysis — what is it?	The first phase consumes ATP to phosphorylate and split the six-carbon sugar, and the second recovers more ATP from the two three-carbon products. Phosphorylation traps the sugar in the cell and destabilizes it for cleavage, so spending ATP early is what makes the later yield possible.
Glyceraldehyde 3-phosphate dehydrogenase step — what is it?	The oxidation that reduces NAD+ and captures the energy as a high-energy acyl phosphate. It is where glycolysis produces its reducing equivalents, which is why the pathway stalls without a way to regenerate NAD+.
Fructose entry into glycolysis — what is it?	Fructose enters below the main regulatory step, being split into three-carbon units after phosphorylation in the liver. Bypassing phosphofructokinase-1 means fructose metabolism is not slowed by high energy charge the way glucose is.
Pyruvate dehydrogenase complex — what is it?	A multi-enzyme assembly using thiamine pyrophosphate, lipoic acid, coenzyme A, FAD, and NAD+ to convert pyruvate to acetyl CoA. The reaction is irreversible, which is why fatty acids cannot be converted back into glucose in humans.
Anaplerotic reactions — what is it?	Reactions replenishing citric acid cycle intermediates that have been withdrawn for biosynthesis. The cycle is catalytic, so removing an intermediate slows every subsequent turn until it is replaced.
Respiratory chain complexes — what is it?	Four membrane complexes, with complexes I, III, and IV pumping protons and complex II feeding electrons in without pumping. Because complex II does not pump, electrons entering there yield less ATP than those entering at complex I.
Uncoupling proteins — what is it?	Inner membrane proteins allowing protons to return to the matrix without passing through ATP synthase. The gradient's energy is released as heat instead of ATP, which is the basis of non-shivering thermogenesis in brown adipose tissue.
Gluconeogenesis — what is it?	Synthesis of glucose from pyruvate, lactate, glycerol, and glucogenic amino acids, mainly in the liver. It is not simply reversed glycolysis, because three glycolytic steps are irreversible and must be bypassed.
Glycogenesis — what is it?	Glycogen synthesis, in which glucose is activated as UDP-glucose and added by glycogen synthase, with a branching enzyme forming alpha-1,6 links. Activation as a uridine nucleotide is what makes addition thermodynamically favourable.
Lipolysis — what is it?	Hydrolysis of stored triacylglycerol into fatty acids and glycerol by hormone-sensitive lipase and associated enzymes.
Oxidation of odd-chain fatty acids — what is it?	The final cycle yields propionyl CoA, which is converted through methylmalonyl CoA to succinyl CoA. Succinyl CoA is a citric acid cycle intermediate, so the three-carbon remnant of an odd-chain fatty acid is glucogenic while the rest is not.
Acetyl-CoA carboxylase — what is it?	The committed and rate-limiting step of fatty acid synthesis, forming malonyl CoA using biotin and ATP.
HMG-CoA reductase step — what is it?	The rate-limiting and committed step of cholesterol synthesis, reducing HMG-CoA to mevalonate using NADPH. The same HMG-CoA intermediate appears in ketogenesis, but that pathway is mitochondrial while cholesterol synthesis is cytosolic.
Transamination — what is it?	Transfer of an amino group from an amino acid to a keto acid, producing a new amino acid and a new keto acid. It is freely reversible and conserves nitrogen, so it redistributes amino groups rather than removing them.
Urea cycle — what is it?	The hepatic pathway converting ammonia into urea for excretion, spanning mitochondrion and cytosol. The two nitrogen atoms of urea come from different sources, one from free ammonia and one from aspartate.
Glucogenic and ketogenic amino acids — what is it?	Glucogenic skeletons enter as pyruvate or a citric acid cycle intermediate, ketogenic ones as acetyl CoA or acetoacetyl CoA. Only leucine and lysine are purely ketogenic, and because acetyl CoA cannot become glucose, only the glucogenic group supports gluconeogenesis.
Purine synthesis — what is it?	Stepwise construction of the base directly onto a ribose phosphate scaffold, so the nucleotide is built rather than assembled from a free base. It is expensive in ATP and in one-carbon units from folate, which is why the salvage pathway carries most of the load in resting cells.
Absorptive state — what is it?	The hours after a meal, when insulin is high and the body stores incoming fuel as glycogen, triacylglycerol, and protein. Glucose is the dominant fuel for every tissue during this window, so fatty acid oxidation is suppressed rather than merely unnecessary.
Metabolic actions of insulin — what is it?	Promotes glucose uptake in muscle and adipose tissue, glycogen and fatty acid synthesis, and protein synthesis, while suppressing lipolysis and gluconeogenesis. It is the only hormone that lowers blood glucose, which is why its actions are described as anabolic across every fuel class at once.
Liver as the metabolic hub — what is it?	The organ receiving portal blood first and holding the enzymes for gluconeogenesis, ketogenesis, urea synthesis, and lipoprotein assembly. It buffers the composition of blood leaving it, so other tissues see a far steadier supply than the gut delivers.
Chemical classes of hormones — what is it?	Peptide and protein hormones, steroid hormones, and amino acid derivatives. Solubility follows the class, and solubility decides whether the hormone needs a surface receptor and whether it travels bound to a carrier protein.
Tropic hormones — what is it?	Hormones whose target is another endocrine gland rather than a non-endocrine tissue. They create the layered feedback structure, so removing the target gland raises the tropic hormone as feedback is lost.
Column chromatography — what is it?	Separation of a mixture passed through a packed column, with components emerging at different times according to how strongly they interact with the packing. Every chromatographic method is this one idea with a different basis of interaction, so identifying the basis predicts the elution order.
Affinity chromatography — what is it?	Separation using a ligand bound to the column that binds only the target protein. It can purify a protein in one step because selectivity comes from biological recognition rather than from a bulk property.
SDS-PAGE — what is it?	Gel electrophoresis in which a detergent denatures proteins and coats them with negative charge proportional to length. Uniform charge-to-mass ratio removes charge and shape as variables, so migration reports size alone.
Two-dimensional gel electrophoresis — what is it?	Isoelectric focusing in one direction followed by SDS-PAGE at right angles to it. Combining two independent properties resolves far more proteins than either alone, which is why it was the original proteomics workhorse.
Edman degradation — what is it?	Sequential removal and identification of one residue at a time from the amino terminus. It reads only a limited stretch before yields decay, and it fails on a blocked amino terminus, which is why long sequences are obtained another way.
Spectrophotometry and the Beer-Lambert relationship — what is it?	Absorbance is proportional to concentration, path length, and the molar absorptivity of the substance. It makes concentration measurable without consuming the sample, and it underlies almost every continuous enzyme assay.
Immunoprecipitation — what is it?	Capture of a target protein from a mixture using an antibody attached to a solid support. Partners bound to the target come down with it, which is how protein interactions are demonstrated in a cell extract.
Southern blot — what is it?	Transfer of size-separated DNA to a membrane, detected with a labelled nucleic acid probe. It detects a specific sequence within a complex genome, and the pattern of bands reports restriction site differences between individuals.
Sanger dideoxy sequencing — what is it?	Sequencing by chain termination, using dideoxynucleotides that lack the 3' hydroxyl needed to extend further. Termination is random and the fragments are separated by size, so the ladder read from smallest upward gives the sequence.
Cloning vector — what is it?	A DNA molecule able to replicate independently and carry an inserted fragment, usually a plasmid or a viral vector.
Site-directed mutagenesis — what is it?	Deliberate alteration of a chosen codon to test what a particular residue contributes. It converts a structural hypothesis into a testable prediction, which is how catalytic residues are confirmed.
Penetrance — what is it?	The proportion of individuals carrying a genotype who show any of the associated phenotype. Expressivity, which is about degree rather than presence.
Mosaicism — what is it?	The presence of two or more genetically different cell populations in one individual, arising from a mutation after fertilization. Whether the change is transmitted depends on whether the germ line is involved, so somatic and germline mosaicism differ in consequence.
Autosomal recessive inheritance pattern — what is it?	A trait appearing in siblings without appearing in the parents, affecting both sexes about equally. Two unaffected carriers are the usual parents, which is why the pattern looks like the trait skipped a generation.
Compound heterozygote — what is it?	An individual carrying two different mutant alleles at the same locus rather than two copies of the same one. The phenotype can be intermediate or unusual, so a recessive condition need not mean two identical alleles.
Loss-of-function mutation — what is it?	A change reducing or abolishing the activity of a gene product. It is usually recessive, because one working copy commonly makes enough product.
Haploinsufficiency — what is it?	A situation in which one working copy of a gene does not produce enough product for the normal phenotype. It explains how a loss-of-function change can nonetheless behave as dominant.
Linkage disequilibrium — what is it?	Non-random association of alleles at nearby loci, so particular combinations occur more often than chance would give. It decays with distance and with generations, so its extent estimates how recently a variant arose.
Consanguinity and homozygosity — what is it?	Mating between relatives raises the chance that offspring inherit two copies of an allele from a shared ancestor. It changes genotype frequencies toward homozygosity without changing allele frequencies, which is why it violates a Hardy-Weinberg assumption.
Resting membrane potential — what is it?	The steady negative interior voltage of an unstimulated neuron, set mainly by potassium permeability and maintained by the sodium-potassium pump. The membrane is far more permeable to potassium than to sodium at rest, so resting potential sits near the potassium equilibrium value.
Removal of neurotransmitter from the synapse — what is it?	Termination by enzymatic degradation, reuptake into the presynaptic terminal, or diffusion away. Without removal the receptor stays occupied, so the mechanism of clearance sets how briefly a synapse can signal.
Sympathetic and parasympathetic compared — what is it?	Sympathetic fibres leave the thoracic and lumbar cord with short preganglionic and long postganglionic neurons. Parasympathetic fibres leave the brainstem and sacral cord with the opposite arrangement. The short sympathetic preganglionic fibres synapse in a chain near the cord, which lets one signal spread widely, while parasympathetic ganglia sit on the target organ and act locally.
Excitation-contraction coupling — what is it?	The sequence from membrane depolarization through calcium release from the sarcoplasmic reticulum to exposure of binding sites on the thin filament. Calcium is the link between an electrical event and a mechanical one, which is why contraction stops when it is pumped back.
Cardiac conduction system — what is it?	Impulse arising in the sinoatrial node, delayed at the atrioventricular node, then spreading through the bundle branches and Purkinje fibres. The delay lets the atria empty before the ventricles contract, so timing rather than speed is the point of that step.
Determinants of cardiac output — what is it?	The product of heart rate and stroke volume, with stroke volume set by preload, afterload, and contractility. Separating the three explains why the same output can be reached in very different ways.
Blood composition — what is it?	Plasma with erythrocytes, leukocytes, and platelets, all arising from haematopoietic stem cells in marrow. Mature erythrocytes have no nucleus and no mitochondria, which is why they cannot repair themselves or use the oxygen they carry.
Alveolar gas exchange — what is it?	Diffusion of oxygen and carbon dioxide across the thin alveolar and capillary walls, driven by partial pressure differences. Rate depends on surface area, membrane thickness, and the pressure gradient, so thickening the barrier impairs exchange without changing the gradient.
Nephron segments — what is it?	Glomerulus and Bowman capsule, proximal convoluted tubule, loop of Henle, distal convoluted tubule, and collecting duct. Each segment has a distinct permeability and transporter set, so knowing the segment predicts what is being moved.
Countercurrent multiplier — what is it?	The loop of Henle arrangement in which a water-permeable descending limb and a salt-transporting, water-impermeable ascending limb build a medullary gradient. The gradient is what makes concentrated urine possible, so loop length predicts an animal's ability to conserve water.
Renal handling of acid and base — what is it?	Reclamation of filtered bicarbonate and excretion of hydrogen ions buffered by phosphate and ammonia. It acts over hours to days, complementing the respiratory response that acts in minutes.
Pancreatic secretion — what is it?	Enzymes released as inactive zymogens together with a bicarbonate-rich fluid. Bicarbonate raises duodenal pH into the range where pancreatic enzymes work, so the two components are useless apart.
Clonal selection — what is it?	Expansion of the few lymphocytes whose receptors happen to fit an antigen, from a repertoire generated before exposure. The repertoire is built by random recombination in advance, so the antigen selects rather than instructs.
Hormonal control of the menstrual cycle — what is it?	Follicle-stimulating and luteinizing hormones driving follicular development and ovulation, with estrogen and progesterone feeding back. Estrogen feedback switches from negative to positive before ovulation, which is what produces the luteinizing hormone surge.
Gastrulation and germ layers — what is it?	Rearrangement producing ectoderm, mesoderm, and endoderm. Every tissue traces to one of the three, so knowing the layer predicts what a structure becomes.
Fetal circulatory shunts — what is it?	Three diversions carrying blood past the liver and lungs before birth, closing after the first breaths. The lungs are fluid-filled and non-functional before birth, so bypassing them is the efficient arrangement until they inflate.

Frequently asked

Why is the deck weighted toward biochemistry?

Because that is where a definition and its consequence come apart most sharply. Amino acid chemistry, kinetics, and metabolic regulation carry 204 of the 350 cards, and they are the areas where a passage can hand you a plot and expect you to read a mechanism off it rather than recall a fact.

What is on each card?

A term on the front. On the back, a definition on all 350, and on 313 the line that makes it usable, most often the consequence that a question would actually turn on. Where two ideas are routinely swapped, the card names the other one and says what separates them. Each line is labeled, so the back reads as a short structured answer.

Does it cover the experimental and laboratory questions?

Yes, as its own block of 40 cards: chromatography by size, charge and affinity, the gel methods including SDS-PAGE and isoelectric focusing, blots and quantitative PCR, sequencing from Sanger to next-generation, and the structural methods from crystallography to cryo-electron microscopy. Each card says what the method separates by, which is what a passage figure usually depends on.

How does it fit with the Cell Biology Essentials deck?

They are built to sit side by side and share no cards. That deck covers organelles, membranes, transport, the cell cycle, and the pathways of respiration and photosynthesis step by step. This one starts where those leave off, going deeper on protein chemistry, enzyme kinetics, metabolic regulation and integration, laboratory methods, and human organ system physiology.

How is it organized for studying one area at a time?

Every card carries an area tag and a finer sub-area tag, across amino acids and proteins, enzymes, carbohydrates and lipids, nucleic acids, bioenergetics, carbohydrate metabolism, lipid and nitrogen metabolism, metabolic integration, genetics, laboratory methods, and organ systems. Filter by a tag to drill one area, or by the finer tag for a single block such as separation techniques or glycolysis detail.

Can I import the whole deck on the free plan?

Yes. Importing a saved deck runs no new AI generation and does not use your AI allowance, so the free plan imports every card. You can study, edit and delete them afterwards.

Will importing it twice create duplicates?

No. Cards you already have are skipped and only cards added in a revision come through. Including re-imports after deleting it, one official deck can be imported three times per account.

Can I edit the cards after importing?

Yes. Once imported they are your cards: edit either side, delete the ones you already know cold, retag them, or move them into another deck.