preprints.org > physical sciences > chemical physics > doi: 10.20944/preprints202307.1664.v1

Preprint Hypothesis Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 24 July 2023 / Approved: 25 July 2023 / Online: 25 July 2023 (07:43:18 CEST)

Proteins in biological systems function at the interface of single molecule and bulk chemistry and thus provide novel insights into the basic physical chemistry of scaling and emergent phenomena. For example, a binary mechanical model based on the chemistry of muscle contraction unifies molecular mechanics and thermodynamics and provides an explicit solution to the Gibbs paradox. Using the same model system, here I show that chemical activities of molecular states have no effect on chemical kinetics or energetics. Specifically, while the concentration or number of molecules in a molecular state is widely thought to contribute to reaction free energies, here I show that it is not the physical presence of molecules that pushes a reaction forward but the number of microstates, , accessible in a chemical state that pulls a reaction toward equilibrium with an entropic force down an entropic funnel. With the derivation of an entropic contribution to chemical kinetics, I develop a novel chemical kinetic formulation that fully describes the chemical thermodynamics of both equilibrium and non-equilibrium reactions in terms of an a priori system reaction energy landscape.

Entropy, Chemical Thermodynamics, Free Energy, Reaction Energy Landscape, Microstates, Micropathways, Non-Equilibrium, Kinetics, Entropic Funnel

Physical Sciences, Chemical Physics

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