LSM2106 Fundamental Biochemistry
The Complete Exam Bible · Sem 1 AY2026/27LSM2106 Overview
- 4 units
- Semester 1 AY2026/27
- Biology
- Closed book, on site
What this guide covers
LSM2106 Fundamental Biochemistry is a four-unit, graded course at the National University of Singapore. The course sets out to ground students securely in how biomolecules are built and what they do inside a cell, and it uses the organelles themselves as the settings in which that question is asked.
- Where the marks are Three written papers carry 94 of the 100 marks; the laboratory report carries the rest.
- The recurring skill Turn a ratio into a pH, an absorbance into a concentration, a rate into moles per minute.
- The recurring trap A reversed direction word: protonated below the pK, deprotonated above it.
- The laboratory link Each practical measures a quantity a lecture defines, and both are examinable.
How LSM2106 is assessed
| Component | Weight | Format |
|---|---|---|
| First continuous assessment: multiple choice and short answer | 20% | Physical, on site, closed book. 5 Oct 2026, 10.30 to 11.30 am; venue announced separately. |
| Second continuous assessment: multiple choice and short answer | 20% | Physical, on site, closed book. 10 Nov 2026, 12.30 to 1.30 pm; venue announced separately. |
| Final examination: multiple choice and short answer | 54% | Physical, on site, closed book. 26 Nov 2026, 9 am. |
| Practical laboratory report | 6% | Question and answer format; introduction and methodology not required. |
The four published weights sum to 100. The course describes the assessments as physical, on-site and closed book, and states that the components may be subject to minor changes. No pass condition or minimum mark is stated for any component in the course materials available here, so treat that as unstated rather than as confirmed either way and check Canvas. Venue details for the two continuous assessments were still to be announced when these materials were published.
Current LSM2106 dates
| Date | Item | Control |
|---|---|---|
| First continuous assessment | 5 Oct 2026, 10.30 to 11.30 am | |
| Second continuous assessment | 10 Nov 2026, 12.30 to 1.30 pm | |
| Reading week | 14 to 20 Nov 2026 | |
| Final examination | 26 Nov 2026, 9 am |
Dates are as published in the current course schedule published for this offering. Confirm exact deadlines and submission settings in the live LMS.
What LSM2106 covers
Eleven chapters follow the thirteen lectures and three laboratory sessions, from the chemistry of water to the integration of every biomolecule class.
Chemistry of Life and Biochemical Measurement
Water, the four biomolecule classes, SI units, significant figures and the Beer and Lambert relation02pH, Acid Chemistry and Buffer Behaviour
Dissociation constants, the Henderson and Hasselbalch form, electrode calibration, buffer choice and capacity03Amino Acids and Their Ionisation
Backbone and side-chain pK values, titration steps, isoelectric point and net charge at a stated pH04Proteins and Quantitative Protein Estimation
Four levels of organisation, denaturation, ultraviolet estimation and the dye-binding standard curve05Forms and Functions of Enzymes
Transition-state stabilisation, the jobs of an active site, cofactors, coupled assays and activity optima06Enzyme Kinetics and Enzyme Inhibitors
Initial velocity from a progress curve, the saturation constants, double-reciprocal plots and inhibition patterns07Enzymatic Regulation
Allosteric binding, covalent modification, proteolytic activation, enzyme amount and feedback inhibition08Cellular Oxygenation
Hyperbolic and sigmoid binding, the delivered fraction, acid and phosphate modulators, terminal electron acceptance09Carbohydrate Metabolism and Cellular Roles
Anomeric orientation, glycosidic bonds, the central catabolic pathway, carrier regeneration, storage and surface roles10Lipids, Membranes and Nucleic Acids
Chain saturation, bilayer self-assembly, selective permeability, base pairing and absorbance at 260 nanometres11Integrating Biomolecules in Cellular Function
The two conserved energy forms, coupling, compartmentation and how to separate evidence in an integrated answerThis guide follows that arc: thirteen lectures and three laboratory sessions, reorganised into eleven chapters that keep the teaching order and merge only where two consecutive lectures describe the same class of molecule from two angles.
The course begins with the chemistry everything else assumes.
Water and the weak, reversible interactions it makes are what fold a protein and close a membrane; the laboratory manual's opening pages on units, significant figures and light absorption are what make any later claim measurable.
From there the sequence moves through acid chemistry and buffers, amino acids and their ionisation, proteins and how to quantify them, enzymes and their kinetics and regulation, cellular oxygenation, carbohydrates, lipids and membranes, nucleic acids, and finally the integration of all of them.
How the course is assessed
Four components carry the mark.
Two continuous assessments of multiple-choice and short-answer questions are worth 20 per cent each, held on 5 October 2026 from 10.30 to 11.30 am and on 10 November 2026 from 12.30 to 1.30 pm, with venues announced separately. The final examination, in the same multiple-choice and short-answer format, is worth 54 per cent and is sat on 26 November 2026 at 9 am. The laboratory report carries the remaining 6 per cent.
The course describes the assessments as physical, on-site and closed book, and states that the components may be subject to minor changes.
That structure has a clear consequence for how to revise. The two short papers fall during teaching, so the useful unit of revision for them is the fortnight.
The final paper is written after the reading week and is worth more than both combined, so it is the only assessment where connections across the whole course can be tested. Build calculation fluency early, because the first laboratory report needs it in week three, and build cross-topic links late.
What makes this subject tractable
Almost every quantity in the course is measured the same way.
The pH meter reports a potential that depends on hydrogen ion concentration; the spectrophotometer reports absorbance, which is proportional to concentration and to path length. Protein is estimated from absorbance, enzyme activity is followed as a change in absorbance per minute, and strand separation is watched as a rise in absorbance.
Students who treat the three practicals as one instrument applied to four different molecules find that the laboratory work and the written papers stop being separate subjects. Three conversions carry most of the marks lost to arithmetic: a ratio into a pH, an absorbance into a concentration, and an absorbance per minute into moles per minute.
The other recurring source of lost marks is a reversed direction word.
A group is protonated below its own pK and deprotonated above it; a competitive inhibitor raises the apparent Michaelis constant and leaves the maximum velocity alone; falling pH lowers the oxygen affinity of the carrier. Each of these is one sentence, and each of them is worth writing out before the calculation rather than after it.
Reading a concentration off an absorbance
- 3Convert the one per cent figure into absorbance per mg per mL.
- 2Divide the reading by that figure and name the assumption.
Key terms
- Absorbance
- The logarithm of the ratio of incident to transmitted light. It has no units and is proportional to the concentration of the absorbing species and to the path length of the cell.
- pK
- The negative logarithm of an acid dissociation constant, and therefore the pH at which the protonated and deprotonated forms of a group are equally abundant.
- Buffer
- A mixture of a weak acid and its conjugate base, which resists a change in pH by converting one form into the other as acid or base is added.
- Isoelectric point
- The pH at which a molecule carries no net charge, obtained by averaging the two pK values that bracket the electrically neutral species.
- Denaturation
- Loss of the folded structure of a protein while its sequence of residues survives, since only the sequence is held by covalent bonds.
- Initial velocity
- The rate of an enzyme-catalysed reaction at the instant it starts, taken as the gradient of the progress curve at time zero.
- Michaelis constant
- The substrate concentration at which an enzyme works at half its maximum velocity. It does not depend on how much enzyme is present.
- Cooperativity
- Interaction between binding sites on a multi-subunit protein, so that occupying one site changes the readiness of the others and the response becomes sigmoid.
- Amphipathic
- Carrying a water-attracting and a water-excluding region in one molecule, which is what drives phospholipids to form a bilayer without any enzyme.
LSM2106 FAQ
How is this course assessed, and what is each component worth?
Four components make up the mark. Two continuous assessments of multiple-choice and short-answer questions carry 20 per cent each, the final examination in the same format carries 54 per cent, and the laboratory report carries 6 per cent. The course describes these as physical, on-site and closed book, and notes that components may be subject to minor changes, so confirm the current details on Canvas.
When is the final examination held?
The course materials give 26 November 2026, a Thursday, at 9 am, after the reading week that runs from 14 to 20 November. The two continuous assessments fall earlier, on 5 October and 10 November. Venue information is announced separately, and both continuous assessment entries were listed with venues still to be confirmed, so check Canvas for the current arrangements.
Is there a hurdle or minimum mark on any component?
No pass condition or minimum mark for any individual component appears anywhere in the course materials available here. That is not the same as a statement that none exists, so treat it as unstated rather than as absent and confirm the current requirements on Canvas before relying on either reading.
What mathematics does this course actually require?
Arithmetic rather than advanced mathematics, but applied carefully. You need logarithms for pH and pK work, proportional reasoning for the absorbance relation, reciprocals and straight-line fitting for the kinetic plots, and confident unit conversion throughout. The differentiation involved is limited to taking the gradient of a fitted quadratic at the origin to obtain an initial velocity.
How do the three practicals relate to the written papers?
Each practical measures a quantity that a lecture defines, so the relations are examinable in both places. The buffer practical uses the acid equation from the pH lecture, the protein practical uses the absorption law from the introductory material, and the kinetics practical uses the saturation and double-reciprocal relations from the kinetics lecture.
Treating the manual as separate reading loses marks in the written papers, not only in the report.
What is the laboratory report expected to contain?
The manual specifies a question-and-answer format, with introduction and methodology not required. Raw data go in captioned tables, plots carry figure captions and proper annotation, and the questions in the manual are answered concisely using your own processed data. Units and significant figures are part of the assessment rather than presentation details.
Which topics are worth the most revision time?
The enzyme block, because kinetics and inhibition span a lecture, a practical and a large share of the calculation questions, and the acid and buffer block, because its reasoning reappears in amino acid charge, protein stability and oxygen affinity. Both reward practice rather than reading, since their marks come from conversions and direction words rather than from recall.
How to study for the exam
Work the arithmetic early and the connections late. In the first fortnight, rehearse the three conversions this course keeps asking for until they are automatic: a concentration ratio into a pH, an absorbance into a concentration, and an absorbance change per minute into moles per minute.
Each of the two continuous assessments tests recent material under time pressure, so revise in fortnights and rebuild the relevant curve from memory rather than rereading notes. For the final paper, which is the only assessment written after all thirteen lectures, practise tracing one observation across several chapters and stating what each piece of evidence alone establishes before combining them.
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