Dive into the catalytic logic and dynamic balance that underpins life’s chemistry with Gwenin’s 6-lecture modular series. This companionable journey explores enzyme kinetics, reaction rates, and chemical equilibrium, perfect for learners, educators, and science communicators.
Lecture 1: Enzyme-Catalysed Reactions and Rate Dependence – 03/03/2026
Why This Series Matters:
Enzymes accelerate reactions with elegance, and understanding how factors like substrate concentration, temperature, and pH affect activity is essential for biochemistry, pharmacology, and physical chemistry. Mastering reaction equilibria and Le Chatelier’s Principle allows prediction and manipulation of chemical systems in both lab and real-world contexts.
Lecture Overview:
- Enzyme-Catalysed Reactions & Rate Dependence – ES complexes, reaction velocity, saturation effects
- Michaelis-Menten Kinetics – Km, Vmax, and catalytic efficiency
- Experimental Determination of Km & Vmax – Measuring enzyme activity, plotting Michaelis-Menten & Lineweaver-Burk data
- Environmental Effects – Temperature, pH, denaturation, optimum conditions
- Reaction Equilibria & Dynamic Balance – Reversible reactions, equilibrium constants, concentration changes
- Le Chatelier’s Principle & Equilibrium Shifts – Predicting system responses to concentration, pressure, temperature, and volume
Features & Learning Outcomes:
- Live links to trusted resources (Khan Academy, ChemLibreTexts, RSC, Nature Education)
- Outreach-ready formatting for flashcards, handouts, or teaching posts
- Modular design for standalone study or sequential learning
- Model enzyme-substrate interactions and reaction velocities
- Analyse experiments and predict environmental effects
- Apply equilibrium expressions and Le Chatelier’s Principle to real-world systems
Explore the full archive at:
ScienceDeconvolution.com
Each lecture is freely available online, with optional PDFs (£1 per lecture) including quizzes supporting remixing and teaching.
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