Szeged Oral Entrance Exam: What They Ask, with Practice Questions

• Open with your real reason in one sentence; the examiner wants yours, not a textbook one.
• Back it with one specific experience you actually had (a job, volunteering, a family situation, something you read) and what it showed you.
• Show you know the reality of the work: long training, responsibility, hard days, not only the rewarding parts.
• Link the reason to qualities you can demonstrate, such as patience, curiosity or working in a team, with a brief example.
• Keep it to one or two minutes and avoid stock phrases like "I have always wanted to help people" unless you can say why.

Likely follow-up: What do you think will be the hardest part of being a doctor for you personally?

• State what drew you to this programme: a six-year medical degree taught in English, in Szeged, Hungary.
• You may mention that the school is named after Albert Szent-Györgyi, who won the 1937 Nobel Prize in Physiology or Medicine for work including vitamin C while at Szeged University, if it genuinely matters to you.
• Only quote facts you have checked yourself on the university's own website; never guess at rankings, numbers or details.
• Give your honest practical and personal reasons (studying in English, living abroad, cost, recommendations from people you know) without apologising for them.
• Show you have thought about living in a new country: independence, a new culture, and willingness to learn some Hungarian for everyday life.

Likely follow-up: How do you expect to cope with living away from home in a country whose language you do not yet speak?

• Choose a real, moderately sized challenge you can talk about calmly: a failed exam, a difficult project, a family or health setback.
• Situation: set the scene in one or two sentences.
• Action: spend most of the time on what you did, step by step, and why.
• Result: say honestly how it turned out, even if only partly successful.
• Reflection: what you learned and how you would use it at medical school.

Likely follow-up: If the same thing happened during your first year of medicine, what would you do differently?

• Describe the methods you really use, not the ones you think sound best.
• Name concrete techniques if you use them, such as testing yourself (active recall), spacing reviews over days, or past-paper practice.
• Explain how you organised your preparation: a timetable, the topic list, how you found and fixed weak areas.
• Admit what did not work and what you changed; it shows you can adapt.
• Finish with how you plan to handle the much larger volume of a medical course.

Likely follow-up: Which topic on the syllabus did you find hardest, and how did you get to grips with it?

• Start with the basics you are sure of: a six-year medical programme taught in English at Szeged, in Hungary.
• Add any detail you have read on the university's own pages, and say where you read it.
• If you describe the usual shape of a medical degree (basic sciences first, then clinical training), make clear you mean medical degrees in general.
• Be honest about what you do not know yet, and say what you would like to find out.
• Connect it to yourself: which part of the course you are most looking forward to, and why.

Likely follow-up: Which subject in the early years do you expect to find most demanding, and why?

• Pick something you have actually read, and name where you read it (newspaper, journal, reliable website).
• Summarise it in two or three plain sentences: what happened or what was found.
• Give both sides, or the limits of the evidence, rather than only your opinion.
• Explain why it matters for patients or doctors.
• Do not quote figures you are not sure of; it is better to say "roughly" or "I don't remember the exact number".

Likely follow-up: What would you need to know before deciding whether that finding should change how doctors treat patients?

• Enzymes are biological catalysts, almost all proteins; the substrate binds the active site to form an enzyme–substrate complex (induced fit).
• They lower activation energy by stabilising the transition state, holding substrates in the right orientation and straining bonds; they do not change ΔG or the position of equilibrium.
• Activity depends on temperature and pH (each enzyme has an optimum; too much heat denatures it), and on substrate and enzyme concentration.
• Competitive inhibitors bind the active site and can be outcompeted by more substrate; non-competitive inhibitors bind elsewhere and lower the maximum rate.
• Cells also regulate enzymes allosterically and by feedback inhibition (ATP inhibits phosphofructokinase), by covalent modification such as phosphorylation, and by making inactive precursors (trypsinogen to trypsin).
• Many enzymes need cofactors: metal ions or coenzymes such as NAD⁺.

Likely follow-up: How do competitive and non-competitive inhibitors change Km and Vmax?

• Glycolysis in the cytoplasm: glucose is split into 2 pyruvate, with a net gain of 2 ATP and 2 NADH; no oxygen is needed.
• In the mitochondrial matrix pyruvate dehydrogenase converts each pyruvate to acetyl-CoA, releasing CO₂ and making NADH.
• The citric acid cycle oxidises each acetyl-CoA to 2 CO₂, producing 3 NADH, 1 FADH₂ and 1 GTP (or ATP) per turn; two turns per glucose.
• NADH and FADH₂ pass electrons along the electron transport chain in the inner mitochondrial membrane; oxygen is the final acceptor and forms water.
• The energy released pumps protons into the intermembrane space; they flow back through ATP synthase, which makes most of the ATP (chemiosmosis).
• Total yield is about 30–32 ATP per glucose (older books say 36–38).

Likely follow-up: What happens to pyruvate when there is no oxygen, and why does the cell bother?

• Transcription in the nucleus: RNA polymerase binds the promoter and reads the template strand 3′→5′, building mRNA 5′→3′.
• In eukaryotes the pre-mRNA is processed: a 5′ cap, a poly-A tail, and splicing that removes introns and joins exons; the mRNA then leaves through the nuclear pores.
• Translation on ribosomes in the cytoplasm starts at the AUG start codon (methionine); each tRNA, charged with its amino acid by an aminoacyl-tRNA synthetase, pairs its anticodon with a codon.
• The ribosome moves along the mRNA through its A, P and E sites, and its rRNA catalyses the peptide bonds; a stop codon (UAA, UAG, UGA) brings in a release factor and ends it.
• The genetic code is a triplet code: 64 codons, 61 for amino acids and 3 stops; it is degenerate, unambiguous and almost universal.

Likely follow-up: How does a bacterium switch genes on and off, for example the lac operon?

• Mitosis is one division giving two genetically identical cells with the same chromosome number (diploid in human body cells); it serves growth and repair.
• Its phases are prophase, metaphase, anaphase and telophase, followed by cytokinesis; in anaphase sister chromatids separate.
• Meiosis is two divisions after one round of DNA replication, giving four haploid, genetically different cells; in humans it makes gametes in the gonads.
• Meiosis I is the reduction division: homologous chromosomes pair, cross over at chiasmata in prophase I, and separate.
• Meiosis II resembles mitosis and separates sister chromatids.
• Variation comes from crossing over, independent assortment of homologues, and random fertilisation.

Likely follow-up: What is nondisjunction, and which conditions can it cause?

• Fluid mosaic model: a phospholipid bilayer with hydrophilic heads outside and hydrophobic tails inside, plus cholesterol, proteins and surface carbohydrates (glycocalyx).
• Simple diffusion: small non-polar molecules such as O₂ and CO₂ cross directly, down their concentration gradient, with no ATP.
• Facilitated diffusion through channels (ion channels, aquaporins) or carriers (GLUT glucose transporters), still down the gradient; osmosis is the diffusion of water.
• Primary active transport uses ATP directly: the Na⁺/K⁺-ATPase moves 3 Na⁺ out and 2 K⁺ in.
• Secondary active transport uses an existing gradient: SGLT1 brings glucose into gut cells together with Na⁺.
• Large particles move in vesicles: endocytosis (phagocytosis, pinocytosis, receptor-mediated uptake such as LDL) and exocytosis.

Likely follow-up: What happens to a red blood cell placed in a hypotonic solution, and in a hypertonic one?

• The resting potential is about −70 mV, inside negative: the Na⁺/K⁺ pump keeps K⁺ high inside and Na⁺ high outside, and the resting membrane is mainly permeable to K⁺, which leaks out.
• A stimulus depolarises the membrane; if it reaches threshold (about −55 mV), voltage-gated Na⁺ channels open.
• Na⁺ rushes in and the inside becomes positive, peaking around +30 to +40 mV; it is all-or-none.
• Na⁺ channels inactivate and voltage-gated K⁺ channels open; K⁺ flows out and repolarises the membrane, briefly overshooting into hyperpolarisation.
• The refractory period stops the impulse going backwards; in myelinated axons it jumps between nodes of Ranvier (saltatory conduction), which is faster.

Likely follow-up: What happens when the action potential reaches the synapse?

• In the glomerulus, blood pressure filters plasma into Bowman's capsule, about 180 L a day; cells and large proteins stay in the blood.
• The proximal tubule reabsorbs about two thirds of the Na⁺ and water and almost all glucose and amino acids.
• In the loop of Henle the descending limb is permeable to water, while the thick ascending limb pumps out Na⁺, K⁺ and Cl⁻ but is impermeable to water; this builds a salt gradient in the medulla (countercurrent multiplier).
• In the distal tubule and collecting duct aldosterone increases Na⁺ reabsorption and K⁺ secretion.
• ADH from the posterior pituitary inserts aquaporins into the collecting duct, so water is drawn into the salty medulla and the urine is concentrated; with little ADH the urine is dilute.
• The result is about 1.5 L of urine a day.

Likely follow-up: How does the renin–angiotensin–aldosterone system respond to a fall in blood pressure?

• Both are adaptive immunity: specific, slower the first time, and with memory, unlike innate immunity.
• Humoral immunity is based on B lymphocytes: once activated (usually with T-helper help) they become plasma cells that secrete antibodies.
• Antibodies neutralise toxins and viruses, coat pathogens for phagocytosis (opsonisation), clump them and activate complement; they mainly deal with extracellular threats.
• Cellular immunity is based on T lymphocytes, which mature in the thymus and recognise antigen presented on MHC molecules.
• Helper T cells (CD4) recognise MHC II on antigen-presenting cells and release cytokines; cytotoxic T cells (CD8) recognise MHC I on infected or tumour cells and kill them with perforin and granzymes.
• Both leave memory cells behind.

Likely follow-up: How does vaccination use this, and why is the second response faster and stronger?

• The motor neuron releases acetylcholine at the neuromuscular junction; it binds nicotinic receptors and depolarises the muscle fibre.
• The action potential spreads along the sarcolemma and down the T-tubules, and the sarcoplasmic reticulum releases Ca²⁺.
• Ca²⁺ binds troponin, which moves tropomyosin and uncovers the myosin-binding sites on actin.
• Cross-bridge cycle: the myosin head binds actin, performs the power stroke and releases ADP and Pi; a new ATP detaches it, and hydrolysing that ATP re-cocks the head.
• Thin filaments slide over thick ones, so the sarcomere, the I band and the H zone shorten while the A band stays the same length.
• Relaxation: acetylcholinesterase breaks down acetylcholine and Ca²⁺ is pumped back into the sarcoplasmic reticulum, which also uses ATP.

Likely follow-up: Why do muscles become rigid after death (rigor mortis)?

• Fasting blood glucose is normally kept at roughly 4–6 mmol/L by negative feedback.
• After a meal, β cells in the islets of Langerhans release insulin.
• Insulin increases glucose uptake into muscle and fat (GLUT4), promotes glycogen synthesis in liver and muscle and fat storage, and suppresses glucose release from the liver.
• When glucose falls, α cells release glucagon, which makes the liver break down glycogen (glycogenolysis) and make new glucose (gluconeogenesis).
• Adrenaline, cortisol and growth hormone also raise blood glucose, especially in stress or fasting; insulin is the only hormone that lowers it.

Likely follow-up: What is the difference between type 1 and type 2 diabetes?

• Law of segregation: each individual has two alleles of a gene, which separate into different gametes.
• Law of independent assortment: alleles of different genes assort independently (true for genes on different chromosomes, not for closely linked ones).
• A dominant allele shows in the heterozygote; crossing two heterozygotes (Aa × Aa) gives a 3:1 phenotype and 1:2:1 genotype ratio.
• X-linked recessive traits, such as haemophilia A or red–green colour blindness, mostly affect males, who have only one X chromosome.
• A carrier mother and an unaffected father: half the sons are affected and half the daughters are carriers.
• An affected father passes his X to all his daughters (carriers) and to none of his sons, so there is no father-to-son transmission.

Likely follow-up: Looking at a family tree, how would you recognise autosomal dominant inheritance?

• Individuals in a population vary, and much of that variation is heritable.
• More offspring are produced than can survive, so there is competition for limited resources.
• Individuals with traits better suited to the environment survive and reproduce more, passing those traits on.
• Over many generations allele frequencies change and populations become adapted; with isolation, new species can form.
• Example: antibiotic resistance, where resistant bacteria survive treatment and multiply.
• Darwin did not know about genes; the modern synthesis combined his theory with Mendelian genetics.

Likely follow-up: How might life have begun, and what did the Miller–Urey experiment show?

• The nucleus holds protons (positive) and neutrons (neutral); electrons (negative, about 1/1836 of a proton's mass) occupy orbitals around it.
• Atomic number Z is the number of protons; mass number is protons plus neutrons; isotopes differ in neutron number.
• Principal quantum number n (1, 2, 3 …) gives the shell, its energy and size; azimuthal quantum number l (0 to n−1, i.e. s, p, d, f) gives the orbital's shape.
• Magnetic quantum number mₗ (−l to +l) gives the orbital's orientation; spin quantum number mₛ is +½ or −½.
• Pauli exclusion principle: no two electrons share all four numbers, so an orbital holds at most two, of opposite spin.
• Orbitals fill by the Aufbau principle and Hund's rule, e.g. carbon is 1s² 2s² 2p².

Likely follow-up: How many electrons can the n = 3 shell hold, and why?

• Elements are ordered by atomic number; a group shares the same number of outer electrons and similar chemistry, and the period number is the number of occupied shells.
• Across a period, nuclear charge rises while electrons enter the same shell, so atoms get smaller.
• Down a group, extra shells and shielding make atoms larger.
• Ionisation energy rises across a period and falls down a group, for the same reasons.
• Electronegativity rises across a period and up a group; fluorine is the most electronegative element.
• Metallic character therefore falls across a period and rises down a group.

Likely follow-up: Why is a sodium ion smaller than a sodium atom, but a chloride ion larger than a chlorine atom?

• Ionic bonds form by electron transfer between atoms with a large electronegativity difference, usually a metal and a non-metal, giving a lattice such as NaCl.
• Covalent bonds are shared electron pairs; they are polar when the two atoms differ in electronegativity. Metallic bonds are cations in a sea of delocalised electrons.
• A Lewis structure shows the valence electrons as bonding pairs and lone pairs, usually completing an octet.
• VSEPR: electron pairs around the central atom repel and get as far apart as possible; lone pairs repel more than bonding pairs.
• CO₂ is linear (180°), BF₃ trigonal planar (120°), CH₄ tetrahedral (109.5°), NH₃ trigonal pyramidal (about 107°) and H₂O bent (about 104.5°).
• Shape decides polarity: CO₂ is non-polar because its polar bonds cancel, while water is polar.

Likely follow-up: Why is water a liquid at room temperature while hydrogen sulfide, a heavier molecule, is a gas?

• At dynamic equilibrium the forward and reverse rates are equal, so concentrations stay constant although both reactions continue.
• Le Chatelier: if conditions change, the equilibrium shifts in the direction that opposes the change.
• Adding a reactant or removing a product shifts it to the right; raising the pressure of a gas reaction shifts it towards fewer moles of gas.
• Raising the temperature favours the endothermic direction; a catalyst does not shift the equilibrium, it only reaches it faster.
• Example, the Haber process, N₂ + 3H₂ ⇌ 2NH₃, exothermic: high pressure raises the ammonia yield, and low temperature would too but is too slow, so a compromise of about 450 °C with an iron catalyst is used.
• Biological example: CO₂ + H₂O ⇌ H₂CO₃ ⇌ H⁺ + HCO₃⁻ in blood shifts as CO₂ is produced in tissues and breathed out in the lungs.

Likely follow-up: Which of these changes alters the value of the equilibrium constant itself, and why?

• Arrhenius: an acid releases H⁺ in water and a base releases OH⁻.
• Brønsted–Lowry: an acid is a proton donor and a base a proton acceptor, forming conjugate pairs, e.g. NH₃ + H₂O ⇌ NH₄⁺ + OH⁻, where water acts as an acid.
• Lewis: an acid accepts an electron pair and a base donates one, e.g. BF₃ + NH₃; this covers reactions with no protons at all.
• pH = −log₁₀[H⁺] (strictly [H₃O⁺]); at 25 °C water's Kw is 1.0 × 10⁻¹⁴, so neutral pH is 7.
• A strong acid dissociates completely (0.01 mol/L HCl has pH 2); a weak acid only partly, described by Ka.
• Blood is kept at pH 7.35–7.45.

Likely follow-up: What is a buffer, and how does the bicarbonate buffer keep blood pH stable?

• Oxidation is loss of electrons (oxidation number goes up); reduction is gain of electrons (oxidation number goes down): "OIL RIG".
• They always happen together; the oxidising agent is itself reduced and the reducing agent is oxidised.
• Rules: an element on its own is 0; oxygen is usually −2 (−1 in peroxides); hydrogen is usually +1 (−1 in metal hydrides); the numbers add up to the overall charge.
• Example: Zn + Cu²⁺ → Zn²⁺ + Cu; zinc is oxidised from 0 to +2 and copper reduced from +2 to 0.
• Biological example: NAD⁺ is reduced to NADH in glycolysis and the citric acid cycle and re-oxidised in the electron transport chain.

Likely follow-up: What is the oxidation number of manganese in KMnO₄, and of sulfur in H₂SO₄?

• Isomers have the same molecular formula but a different arrangement of atoms.
• Structural isomers differ in connectivity: chain (butane and 2-methylpropane), position (propan-1-ol and propan-2-ol), functional group (ethanol and dimethyl ether, both C₂H₆O).
• Stereoisomers have the same connectivity but a different arrangement in space.
• Cis–trans (geometric) isomerism arises around a C=C double bond, which cannot rotate, e.g. cis- and trans-but-2-ene.
• Optical isomerism: a carbon with four different groups is chiral; its two enantiomers are non-superimposable mirror images that rotate plane-polarised light in opposite directions.
• In biology it matters: proteins are built from L-amino acids and most natural sugars are D-sugars.

Likely follow-up: How many chiral carbons does open-chain glucose have, and what are α and β anomers?

• Alkanes (CₙH₂ₙ₊₂) are saturated, with only C–C and C–H single bonds, so they are fairly unreactive apart from combustion.
• With halogens under UV light they undergo free-radical substitution (initiation, propagation, termination), e.g. CH₄ + Cl₂ → CH₃Cl + HCl.
• Alkenes (CₙH₂ₙ) have a C=C double bond, a σ bond plus a weaker, electron-rich π bond, which attracts electrophiles.
• Their typical reaction is electrophilic addition: hydrogen (with a Ni or Pt catalyst), bromine (bromine water is decolourised, a test for C=C), hydrogen halides, and water with an acid catalyst to give an alcohol.
• Alkenes also polymerise by addition, e.g. ethene to polyethene; alkynes (CₙH₂ₙ₋₂) have a triple bond and can add twice.

Likely follow-up: What is the main product when HBr adds to propene, and why (Markovnikov's rule)?

• The carboxyl group −COOH makes them weak acids (ethanoic acid has a pKa of about 4.8); they form salts with bases and hydrogen-bond strongly.
• Esterification: carboxylic acid + alcohol ⇌ ester + water, a reversible condensation catalysed by acid (concentrated H₂SO₄), e.g. ethanoic acid + ethanol → ethyl ethanoate.
• Acid hydrolysis of an ester is the reverse and is also reversible.
• Hydrolysis with a base (saponification) goes to completion and gives the alcohol and a carboxylate salt; soap is made this way from fats.
• Fats (triglycerides) are esters of glycerol and three fatty acids; an amide forms in the same way from a carboxylic acid and an amine, and the peptide bond is an amide.

Likely follow-up: Why is an amide much less basic than an amine?

• An α-amino acid has a central carbon carrying an amino group, a carboxyl group, a hydrogen and a side chain (R); 20 are standard in proteins.
• All except glycine are chiral, and proteins use the L form.
• At physiological pH they exist mainly as zwitterions (−NH₃⁺ and −COO⁻), so they are amphoteric; the pH at which net charge is zero is the isoelectric point.
• A peptide bond forms by condensation between the carboxyl group of one amino acid and the amino group of the next, releasing water: it is an amide bond.
• The peptide bond has partial double-bond character, so it is planar, does not rotate freely and is usually trans.
• A chain has an N-terminus and a C-terminus, and is broken by hydrolysis with acid or with protease enzymes.

Likely follow-up: What holds a protein together at its primary, secondary, tertiary and quaternary levels of structure?