Molecular Engineering - Intro to Biomedical Engineering

Compute a binomial probability for three folded proteins in a 30-protein system using multiplicity and an unbiased 0.5 probability. Derive 30 choose 3 equals 4060 and a probability near 3.7e-6.

Explore further applications of multiplicity, including how adding molecules affects multiplicity and how multiplicative and additive natural log properties simplify entropy calculations, illustrated with two-molecule cases.

Examine entropy as disorder and its two main forms: statistical entropy S = k_B ln multiplicity and thermodynamic entropy q/T, and how they relate under the second law.

Review the quiz line by line to clarify microstates, multiplicity, and entropy, and apply the statistical entropy relation with k_B and W, plus Kelvin conversions for energy questions.

Analyze entropy and multiplicity via a microstate problem, counting molecular arrangements across energy levels and applying the Boltzmann constant and natural log to compare systems.

Explore Boltzmann and probability by linking multiplicity, entropy, and equilibrium to the Boltzmann distribution. Use partition functions and the Boltzmann constant to compute molecular populations across energy levels.

Explore spontaneous and non-spontaneous reactions, standard free energy, and how free energy governs work, entropy, and equilibrium in thermodynamic cycles.

Learn how delta H, delta S, and delta G relate enthalpy and entropy to Gibbs free energy and spontaneity at constant temperature and pressure.

Examine how free energy drives work, distinguishing expansion work from non expansion work, and relate Gibbs free energy changes to spontaneity and energy sources such as catalysts or ATP.

Explore thermodynamic cycles and the standard free energy change of formation, showing how to determine the final energy of glucose formation from basic building blocks through elementary reactions.

clarifies that at equilibrium entropy is maximal and free energy is minimal. explains when ΔG is negative and differentiates expansion (physical) work from non expansion work.

Explain chemical potential as the energy change from changing particle numbers, driven by gradients and equilibrium, with applications to diffusion, acid-base reactions, protein folding, and the Delta MU equation.

Determine whether a system is at equilibrium by calculating the equilibrium constant from product and reactant concentrations raised to their mole powers, and use the reaction quotient to assess non-equilibrium.

Explore chemical potential and equilibrium by linking K, Q, and mass action ratio to compute delta G from concentrations and standard Gibbs energy, revealing how concentration changes affect spontaneity.

Define acids and bases, show proton donation and acceptance, and introduce conjugate acid-base pairs and the Henderson hostile block equation for pH from equilibrium constants.

Review chemical potential, equilibrium, and free energy, including the equilibrium constant, mass action ratio, and reaction quotient, plus acids, bases, the Henderson Hasselbaink equation, and protein folding driving forces.

Explore reduction potentials and how redox reactions create an electrical signal, using half-reactions and copper and zinc electrodes in copper sulfate and zinc sulfate solutions to power a battery.

Explore how potential differences arise from reduction and oxidation, linking free energy to electrical work and voltage, and visualize voltage with electric field lines.

Balance the silver and zinc half-reactions, apply e = -Δg°/(n f), and determine the standard potential, noting that voltages are not additive and spontaneity follows the computed voltage.

Explore how the Nernst equation updates standard reduction potential E0 to the cell potential using the reaction quotient, RT, the electrons involved, and the Faraday constant.

Quiz review covers oxidation and reduction, oil rig, salt bridges in galvanic cells, hydrogen reference 0.0 V, field lines, and the Nernst equation for Ecell.

Explore binding thermodynamics by defining binding free energy from protein and ligand, and compute it using the association constant with ln(K) times T times R.

Explore how binding free energy and association and dissociation constants relate to affinity and specificity, and learn to calculate the specificity factor to compare ligand binding across receptors.

Explore bound ligand concentration and dissociation and association constants, derive saturation using F = [L]/([L]+Kd), and introduce the scratcher equation for unknown receptor concentrations.

Review biomolecular recognition, affinity and specificity, and binding thermodynamics, covering association and dissociation, binding free energy, lagging concentration, and how drugs bind proteins to impact health care.

Master biomolecular recognition concepts through a quiz review, distinguishing non-examples, calculating free energy of binding, and understanding how protein concentration and polar interactions drive drug binding.

Explore reaction rates, their definitions, symbols, and rate laws; examine stoichiometry and equilibrium constants, and show how collisions, temperature, and concentration determine reaction speed.

Explore activation energy and how temperature, collisions, and concentration influence reaction rates, with the Arrhenius equation guiding rate constants and energy thresholds.

Apply the Arrhenius equation to determine activation energy from rate, temperature, and concentrations in an elementary A + B → C reaction, with a room-temperature example.

Explore how catalysts increase reaction rates by lowering activation energy, increasing collision frequency, and boosting the frequency factor, with enzymes illustrating induced fit to lower the energy barrier.

Review equilibrium free energy and activation concepts through a comprehensive quiz review. Examine how collisions, orientation, and temperature drive reaction rates and the rate-determining step.