Molecular Engineering - Intro to Biomedical Engineering

Explore entropy as a measure of disorder and multiplicity as the number of configurations at given energy levels, and learn how these relate to probability, energy distribution, and practice problems.

Explore how multiplicity informs entropy and probability, and apply binomial and Gaussian distributions to model molecular engineering phenomena, including mean and variance.

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 states and microstates, and how temperature, pressure, and molecule count influence multiplicity and entropy. Use probability and the binomial distribution to count configurations with the same energy.

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.

Compute entropy for each system using the Boltzmann constant 1.38e-23 and the natural log of multiplicities 65 and 100. Then determine the total entropy change by subtracting the two values.

Review energy, entropy, and multiplicity, focusing on micro states and states, and learn how to apply binomial probability to multiplicity and both thermodynamic and statistical entropy.

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.

Explore entropy and energy multiplicity, linking increasing disorder to higher microstate counts. See how heat transfer toward maximum combined entropy drives equilibrium between systems.

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 thermal equilibrium by linking thermodynamic entropy (heat transfer over temperature) with statistical entropy (Boltzmann constant times log multiplicity); at equilibrium no heat flows and entropy change is zero.

Provide a quiz recap of multiplicity and heat transfer, Boltzmann probability, and thermal equilibrium concepts, emphasizing enthalpy, entropy, and temperature changes to prep for the quiz.

Quiz review retraces how multiplicity and entropy rise toward equilibrium, linking microstates arrangements to thermodynamic trends, and clarifies probability of energy levels and thermal equilibrium conditions.

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.

Explore standard free energy, defined by Gibbs energy under standard conditions, and how delta H and delta S determine spontaneity and free energy of formation with additivity.

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.

Review spontaneous versus non spontaneous processes, standard free energy, and free energy work. Understand thermodynamic cycles, enthalpy, Gibbs energy, and non expansion work to prepare for the quiz.

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.

Explore how chemical potential relates to protein folding, linking unfolded and folded states. Understand how amino acid charges, pKa shifts, and enthalpy‑entropy balance drive folding and stabilize the folded protein.

This lecture presents a protein folding example using Gibbs free energy, with 40 residues, hydrogen bond enthalpy of -4 kJ/mol, at 300 K, showing it is not spontaneous.

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.

Review key quiz topics on chemical potential, potential difference, mass action ratio, protein folding, and pKa definitions for molecular engineering fundamentals.

Examine oxidation-reduction (redox) reactions, detailing oxidation and reduction processes, reduction potentials, and standard potentials with the Nernst equation. Illustrate with a zinc-copper example and mitochondrial energy production.

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.

Explore standard reduction potential by analyzing half reactions, hydrogen as ground 0 V, and how standard conditions define voltage and free energy in redox reactions.

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.

Review the quiz with key points from the last six lectures on oxidation-reduction reactions, reduction potential, potential difference, standard reduction potentials, half-cell equations, and the Nernst equation.

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 biomolecular recognition through non covalent interactions between proteins and ligands, including hydrogen bonding, metal coordination, and hydrophobic forces, and how these interactions form protein-ligand complexes that lower free energy.

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.

Learn how drugs bind to protein targets, balancing hydrophobic and polar interactions, with lock-and-key or induced-fit mechanisms and entropy loss compensated by the hydrophobic effect and release of protein-bound water.

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 how free energy governs molecular process rates and spontaneous reactions. Link enthalpy, entropy, and Gibbs free energy to predict when reactions proceed.

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 how the order of reaction rates—first, second, and zeroth—depends on concentration and stoichiometry, shaping reaction speed. Examine rate determining steps in multi-step reactions.

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 fundamental concepts of free energy and spontaneity, the second law of thermodynamics, reaction rates and rate constants, reaction orders, activation energy, Arrhenius equation, and catalysts.

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.