Life as Plasmas: Autonomy and Interactivism in-materio

When is a material system a candidate for life at all? We argue that this question is prior to behavior, functional architecture, or computational capacity, and that at root it is one of physical admissibility. We develop a framework in which minimal autonomy, taken in the interactivist sense of normativity grounded in self-maintaining far-from-equilibrium organization, corresponds to a distinct non-equilibrium phase of matter, and we take complex plasmas, a physical and non-biological system, as its in-materio exemplar. We formalize a diagnostic phase-space whose criteria (sustained free-energy throughput, organizational closure, active information maintenance, and regulated noise sensitivity) constitute necessary conditions for life-attribution. We instantiate the diagnostics across contrasting systems and fix the boundaries of the phase space via Bénard convection as a driven baseline lacking closure, and a digital self-replicating soup that carries measured informational heredity while its physical closure remains a structural zero. We demonstrate that plasmas satisfy every admissibility condition for minimal physical autonomy while carrying none of the informational heredity that open-ended evolution requires, sharpening the distinction between physical admissibility and biological sufficiency, and bounding downstream questions of machine sentience.

Multi-state Protein Design with DynamicMPNN

Structural biology has long been dominated by the one sequence, one structure, one function paradigm, yet many critical biological processes - from enzyme catalysis to membrane transport - depend on proteins that adopt multiple conformational states. Existing multi-state design approaches rely on post-hoc aggregation of single-state predictions, achieving poor experimental success rates compared to single-state design. We introduce DynamicMPNN, an inverse folding model explicitly trained to generate sequences compatible with multiple conformations through joint learning across conformational ensembles. Trained on 46,033 conformational pairs covering 75% of CATH superfamilies and evaluated using AlphaFold initial guess, DynamicMPNN outperforms ProteinMPNN by up to 13% on structure-normalized RMSD across our challenging multi-state protein benchmark.