Life uses entropy to crack impossible odds. Here's how. | EoB Ch 2

Cyrus Levinthal identified this paradox in 1969 when studying protein folding mechanisms. Biochemists and molecular biologists confront this problem when explaining how proteins achieve their functional three-dimensional structures.

Albert Einstein and Marian Smoluchowski independently developed the mathematical theory of diffusion in 1905-1906. Jean Perrin’s experiments confirming Brownian motion validated their predictions. Chemists and biologists rely on diffusion principles to understand molecular transport.

Ludwig Boltzmann formulated this statistical interpretation of entropy in the late 19th century. The equation S = k_B ln(Ω) appears carved on his gravestone. Physicists and chemists apply this framework to understand thermodynamic behavior from molecular arrangements.

Rudolf Clausius formulated the modern statement of the second law in 1850. William Thomson (Lord Kelvin) developed complementary formulations. Sadi Carnot’s earlier work on heat engine efficiency provided foundational insights. Physicists, chemists, and engineers apply this law universally.

Josiah Willard Gibbs developed the thermodynamic framework connecting enthalpy to chemical equilibria in the 1870s. Physical chemists and biochemists measure enthalpy changes to quantify molecular interactions. Structural biologists use enthalpy to understand binding affinities and reaction energetics.

Christian Anfinsen demonstrated in the 1960s that protein folding is thermodynamically determined by amino acid sequence. Structural biologists and computational chemists study how conformational entropy influences folding pathways and stability. Molecular dynamics researchers simulate these entropic contributions.

Walter Kauzmann proposed in 1959 that hydrophobic interactions drive protein folding. Physical chemists and structural biologists recognize this as the dominant force organizing protein architecture. Computational chemists model solvent entropy contributions to folding energetics.

Josiah Willard Gibbs formulated this thermodynamic potential in the 1870s to predict reaction spontaneity. Chemists and biochemists use Gibbs free energy as the central criterion for determining reaction feasibility. Metabolic engineers manipulate free energy to optimize biochemical pathways.

Fritz Lipmann elucidated ATP’s role as the universal energy currency in the 1940s, earning the Nobel Prize in 1953. Biochemists study how cells couple ATP hydrolysis to drive otherwise unfavorable processes. Cell biologists examine ATP-dependent molecular machines throughout cellular systems.

Svante Arrhenius developed kinetic theory in 1889, distinguishing reaction rates from thermodynamic favorability. Enzymologists study how catalysts accelerate kinetics without changing thermodynamics. Structural biologists investigate transition states and activation barriers that govern reaction rates.