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Climate change increases fire-favorable weather in forests, but fire trends are also affected by multiple other controlling factors that are difficult to untangle. We use machine learning to systematically group forest ecoregions into 12 global forest pyromes, with each showing distinct sensitivities to climatic, human, and vegetation controls. This delineation revealed that rapidly increasing forest fire emissions in extratropical pyromes, linked to climate change, offset declining emissions in tropical pyromes during 2001 to 2023. Annual emissions tripled in one extratropical pyrome due to increases in fire-favorable weather, compounded by increased forest cover and productivity. This contributed to a 60% increase in forest fire carbon emissions from forest ecoregions globally. Our results highlight the increasing vulnerability of forests and their carbon stocks to fire disturbance under climate change. 

Abstract A generalized understanding of protein dynamics is an unsolved scientific problem, the solution of which is critical to the interpretation of the structure-function relationships that govern essential biological processes. Here, we approach this problem by constructing coarse-grained molecular potentials based on artificial neural networks and grounded in statistical mechanics. For training, we build a unique dataset of unbiased all-atom molecular dynamics simulations of approximately 9 ms for twelve different proteins with multiple secondary structure arrangements. The coarse-grained models are capable of accelerating the dynamics by more than three orders of magnitude while preserving the thermodynamics of the systems. Coarse-grained simulations identify relevant structural states in the ensemble with comparable energetics to the all-atom systems. Furthermore, we show that a single coarse-grained potential can integrate all twelve proteins and can capture experimental structural features of mutated proteins. These results indicate that machine learning coarse-grained potentials could provide a feasible approach to simulate and understand protein dynamics.