Chemkit

Biochem chemistry

Enzyme kinetics (Michaelis–Menten, Lineweaver–Burk), protein–ligand binding, nucleic-acid Tm, and biological buffer preparation.

7 guides 1 calculator 0 cheat sheets

Reading path

Start here. Each guide is a self-contained tutorial with worked examples and cited sources.

  1. Why enzymes plateau: reading v vs [S] curves Michaelis-Menten in words. What Km and Vmax actually mean, and what kcat/Km tells you about a 'perfect' enzyme. 11 min
  2. Reading enzyme inhibition patterns Each inhibition mode leaves a distinct Km/Vmax fingerprint. Match the pattern, extract Ki, watch for irreversibility. 12 min
  3. Physiological buffers: beyond Henderson-Hasselbalch Bicarbonate, phosphate, and protein buffers keep blood pH within 0.05 units. The 20:1 ratio, the open system, and the four ABG disturbances. 12 min
  4. Cooperative binding: hemoglobin and the Hill equation Hemoglobin binds four oxygens, and each binds easier than the last. The Hill equation, MWC states, and the Bohr effect. 12 min
  5. Bioenergetics: ΔG in a metabolic pathway ATP is not the fuel; ΔG is. Every step has a ΔG, and only the sum needs to be negative. How coupling and disequilibrium drive the pathway. 12 min
  6. Electron transport chain: proton gradient to ATP Four complexes drop electrons through a redox staircase to O₂; the released energy pumps protons; ATP synthase turns the gradient back into ATP. 13 min
  7. Membrane transport: passive, facilitated, and active Three transport modes set every ion gradient in every cell. Nernst equation, Na/K-ATPase, secondary active symporters and antiporters, and the physiology that rides them. 12 min

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