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AlphaFold2 revolutionized structural biology with the ability to predict protein structures with exceptionally high accuracy. Its implementation, however, lacks the code and data required to train new models. These are necessary to (1) tackle new tasks, like protein–ligand complex structure prediction, (2) investigate the process by which the model learns and (3) assess the model’s capacity to generalize to unseen regions of fold space. Here we report OpenFold, a fast, memory efficient and trainable implementation of AlphaFold2. We train OpenFold from scratch, matching the accuracy of AlphaFold2. Having established parity, we find that OpenFold is remarkably robust at generalizing even when the size and diversity of its training set is deliberately limited, including near-complete elisions of classes of secondary structure elements. By analyzing intermediate structures produced during training, we also gain insights into the hierarchical manner in which OpenFold learns to fold. In sum, our studies demonstrate the power and utility of OpenFold, which we believe will prove to be a crucial resource for the protein modeling community. OpenFold is a trainable open-source implementation of AlphaFold2. It is fast and memory efficient, and the code and training data are available under a permissive license.

The State of Brain Emulation Report 2025 provides a comprehensive reassessment of the field's progress since Sandberg and Bostrom's 2008 Whole Brain Emulation roadmap. The report is organized around three core capabilities required for brain emulation: recording brain function (Neural Dynamics), mapping brain structure (Connectomics), and emulation and embodiment (Computational Neuroscience). It also identifies ongoing challenges and outlines strategic priorities to help the field move forward.

We identify a substantial pool of technically competent ML research talent (in the low thousands) in companies which offer consulting in machine learning. We systematically searched the internet, global business databases, and conference/paper affiliations for ML consulting firms. Employee LinkedIn resumes were then scored by keyword filters and large-language-model (LLM) classifiers; these signals were combined in a bootstrap probit model to estimate technical ML research talent per firm. A subset of companies also completed a 3-day research and engineering work trial. We screened 2121 organizations and found 403 offering broad ML consulting. Our 50th percentile aggregate estimate of 'highly technical' ML research talent across these organizations was 1121 (80% CI: 252-3165) -- i.e. twice as many as all alumni of the MATS training program. For our work trial 97 companies were approached, 20 applied, 8 were invited to participate, and 5 of 8 received at least a conditional recommendation for technical AI safety work. As of late 2025, no AI model was able to pass the work trial.

Self-supervised pretraining on protein sequences has led to state-of-the art performance on protein function and fitness prediction. However, sequence-only methods ignore the rich information contained in experimental and predicted protein structures. Meanwhile, inverse folding methods reconstruct a protein's amino-acid sequence given its structure, but do not take advantage of sequences that do not have known structures. In this study, we train a masked inverse folding protein language model parameterized as a structured graph neural network. We then show that using the outputs from a pretrained sequence-only protein masked language model as input to the inverse folding model further improves pretraining perplexity. We evaluate both of these models on downstream protein engineering tasks and analyze the effect of using information from experimental or predicted structures on performance.Competing Interest StatementThe authors have declared no competing interest.Footnotes* Added new experiments; put OOD before zero-shot.* https://zenodo.org/record/6573779#.Y3ufU-zMITs

As AI systems become increasingly powerful, the need for safe AI has become more pressing. Humans are an attractive model for AI safety: as the only known agents capable of general intelligence, they perform robustly even under conditions that deviate significantly from prior experiences, explore the world safely, understand pragmatics, and can cooperate to meet their intrinsic goals. Intelligence, when coupled with cooperation and safety mechanisms, can drive sustained progress and well-being. These properties are a function of the architecture of the brain and the learning algorithms it implements. Neuroscience may thus hold important keys to technical AI safety that are currently underexplored and underutilized. In this roadmap, we highlight and critically evaluate several paths toward AI safety inspired by neuroscience: emulating the brain's representations, information processing, and architecture; building robust sensory and motor systems from imitating brain data and bodies; fine-tuning AI systems on brain data; advancing interpretability using neuroscience methods; and scaling up cognitively-inspired architectures. We make several concrete recommendations for how neuroscience can positively impact AI safety.

As AI systems become increasingly powerful, the need for safe AI has become more pressing. Humans are an attractive model for AI safety: as the only known agents capable of general intelligence, they perform robustly even under conditions that deviate significantly from prior experiences, explore the world safely, understand pragmatics, and can cooperate to meet their intrinsic goals. Intelligence, when coupled with cooperation and safety mechanisms, can drive sustained progress and well-being. These properties are a function of the architecture of the brain and the learning algorithms it implements. Neuroscience may thus hold important keys to technical AI safety that are currently underexplored and underutilized. In this roadmap, we highlight and critically evaluate several paths toward AI safety inspired by neuroscience: emulating the brain's representations, information processing, and architecture; building robust sensory and motor systems from imitating brain data and bodies; fine-tuning AI systems on brain data; advancing interpretability using neuroscience methods; and scaling up cognitively-inspired architectures. We make several concrete recommendations for how neuroscience can positively impact AI safety.

AlphaFold2 revolutionized structural biology with the ability to predict protein structures with exceptionally high accuracy. Its implementation, however, lacks the code and data required to train new models. These are necessary to (i) tackle new tasks, like protein-ligand complex structure prediction, (ii) investigate the process by which the model learns, which remains poorly understood, and (iii) assess the model's generalization capacity to unseen regions of fold space. Here we report OpenFold, a fast, memory-efficient, and trainable implementation of AlphaFold2, and OpenProteinSet, the largest public database of protein multiple sequence alignments. We use OpenProteinSet to train OpenFold from scratch, fully matching the accuracy of AlphaFold2. Having established parity, we assess OpenFold's capacity to generalize across fold space by retraining it using carefully designed datasets. We find that OpenFold is remarkably robust at generalizing despite extreme reductions in training set size and diversity, including near-complete elisions of classes of secondary structure elements. By analyzing intermediate structures produced by OpenFold during training, we also gain surprising insights into the manner in which the model learns to fold proteins, discovering that spatial dimensions are learned sequentially. Taken together, our studies demonstrate the power and utility of OpenFold, which we believe will prove to be a crucial new resource for the protein modeling community.Competing Interest StatementM.A. is a member of the Scientific Advisory Boards of Cyrus Biotechnology, Deep Forest Sciences, Nabla Bio, Oracle Therapeutics, and FL2021-002, a Foresite Labs company. P.K.S. is a member of the Scientific Advisory Board or Board of Di- rectors of Glencoe Software, Applied Biomath, RareCyte, and NanoString and is an advisor to Merck and Montai Health.Footnotes* https://github.com/aqlaboratory/openfold* https://registry.opendata.aws/openfold/* https://figshare.com/articles/media/Folding_animations/21561939

In this work we introduce RITA: a suite of autoregressive generative models for protein sequences, with up to 1.2 billion parameters, trained on over 280 million protein sequences belonging to the UniRef-100 database. Such generative models hold the promise of greatly accelerating protein design. We conduct the first systematic study of how capabilities evolve with model size for autoregressive transformers in the protein domain: we evaluate RITA models in next amino acid prediction, zero-shot fitness, and enzyme function prediction, showing benefits from increased scale. We release the RITA models openly, to the benefit of the research community.

We introduce StableLM 2 1.6B, the first in a new generation of our language model series. In this technical report, we present in detail the data and training procedure leading to the base and instruction-tuned versions of StableLM 2 1.6B. The weights for both models are available via Hugging Face for anyone to download and use. The report contains thorough evaluations of these models, including zero- and few-shot benchmarks, multilingual benchmarks, and the MT benchmark focusing on multi-turn dialogues. At the time of publishing this report, StableLM 2 1.6B was the state-of-the-art open model under 2B parameters by a significant margin. Given its appealing small size, we also provide throughput measurements on a number of edge devices. In addition, we open source several quantized checkpoints and provide their performance metrics compared to the original model.

This paper is aimed at discussing a series of energy sustainability solutions proposed by a master class of students in environmental engineering using analytical and visual collaborative tools. The activities described are part of the class “Sustainability and renewable sources” at the University of Modena and Reggio Emilia. Six groups of 3-4 students worked on six energy efficiency and sustainability projects chosen from a remote area of the Apennines in Emilia Romagna. The specificity of the case-study framework allowed the implementation of projects where different sustainability aspects are integrated using tools of transitional thinking: agro-food production, use of renewable energy sources, waste management and social integration were considered. Each group identified the key actors for each project, allowing them to approach sustainability from a multilevel perspective. Net Present Value analyses were applied to evaluate economic viability of each project. Photovoltaic power plants and boilers fueled with local wood are the main renewable energy source identified to promote energy sustainability in each project. As result, the combination of the six works creates a powerful tool to demonstrate possible best practices for remote mountain areas.