Charles Mullins posts molecule stability claim

- Charles Mullins posted on X on June 1, 2026 that light, enzymes and mechanical force can help hold molecules in higher-energy states. - The key scientific point is metastability: molecules can remain in local energy minima, while enzymes change rates and barriers rather than overturning thermodynamics. - Mullins linked references in his June 1 X thread, where readers can review the cited papers and examples.

Charles Mullins said in a June 1 post on X that light, enzymes and mechanical force can stabilize higher-energy molecular structures rather than always driving matter to its lowest-energy state. His thread presented that claim as a challenge to a simplified view of thermodynamics and linked out to papers and examples. The underlying scientific idea is not that thermodynamics has stopped applying. The more established concept is that many materials and molecules can persist in metastable states — local energy minima separated from the lowest-energy state by barriers that slow or prevent relaxation. The chemistry and materials literature describes those states as common, useful and often deliberately accessed in experiments. ### What was Mullins actually claiming? Charles Mullins’ June 1 thread argued that external inputs such as light, enzymatic activity and mechanical force can be used to create or preserve molecular arrangements that sit above the ground state in energy. That framing matches a broad scientific practice: researchers often use energy input or environmental control to reach structures that are not the global minimum but are long-lived enough to study or use. (pubs.rsc.org) The most important distinction is between thermodynamic stability and kinetic persistence. A higher-energy structure can exist for a long time if the pathway down to the lower-energy state is blocked by a sufficiently high barrier. That is the standard meaning of metastability in the literature. ### Does that “challenge thermodynamics”? Georgia Tech’s teaching material on energy and enzymes states that the second law still applies in biological systems, including systems that maintain local order, because they exchange energy and increase entropy in their surroundings. (pubs.rsc.org) In that framework, catalysts and enzymes do not repeal thermodynamics; they alter rates and accessible pathways. That means Mullins’ language is best read as a challenge to the oversimplified slogan that matter always immediately falls to the lowest-energy arrangement, not as evidence that the laws of thermodynamics have been overturned. The literature on metastable phases explicitly treats non-equilibrium, higher-energy states as compatible with thermodynamics when barriers, driving forces and environmental conditions are included. (bioprinciples.biosci.gatech.edu) ### How can light hold a system in a higher-energy state? Nature Materials described “on-demand light-driven metastability” in a 2025 news-and-views article about a long-lived metallic state produced by irradiation in a quantum material. Separate work in molecular systems has shown that photon energy can be stored in metastable photoisomers, which later relax back to the thermodynamically preferred form when triggered. (pubs.rsc.org) Science Advances and Nature Communications papers also describe light as a way to switch, trap or stabilize metastable states and intermediates under controlled conditions. Those are not permanent violations of equilibrium behavior; they are externally driven or kinetically trapped states. ### What do enzymes change? Enzymes are best understood as catalysts that lower activation barriers and reshape reaction pathways, not as agents that rewrite the equilibrium destination by themselves. (nature.com) Georgia Tech’s biochemistry material says a negative or positive Gibbs free energy still governs spontaneity, while catalysts affect how quickly a reaction proceeds. (science.org) Cell and Biophysical Journal papers cited in search results also describe enzymes and protein machines accessing high-energy conformations or generating force during function. Those findings support the narrower claim that biological systems can transiently occupy or exploit higher-energy configurations during catalysis and mechanical work. ### Where does mechanical force fit in? (bioprinciples.biosci.gatech.edu) Mechanical input is a recognized way to reshape an energy landscape. Science and Cell papers describe force, pressure or mechanochemical methods as ways to induce transitions, preserve metastable structures or unfold biomolecules along pathways that would not be reached the same way at equilibrium. In plain terms, force can push a molecule or material over one barrier and into another basin where it remains trapped for some time. (link.aps.org) That is a controllable materials strategy, but it still depends on energy input and kinetics. ### So what is the clean takeaway? The clean takeaway from Mullins’ June 1 thread is that chemistry already has a language for what he is pointing to: metastability, driven systems and kinetic control. (science.org) Light, enzymes and force can all help systems reach or hold higher-energy arrangements under the right conditions. The next step for readers is in the thread itself: Mullins said he linked experimental examples and references on June 1, and those papers are the place to test how broad his claim is and which examples are molecular, biological or materials-specific. (pubs.rsc.org)

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