Best Power Banks Best Smart Rings Routers vs. Modems Choose the Right Laptop Smart Sprinklers Deals Delivered The beleaguered luxury phone maker is pushing the AlphaFold, which has decent specs and comes with Vertu's new Hermes Agent on board, to wealthy would-be buyers. Vertu is a company known for making extraordinarily gaudy smartphones with outdated technology, luxe materials, and eye-watering prices . Now the brand is here to meet the AI moment with its first-ever book-like folding phone, complete with an AI agent on board. The company announced the AlphaFold smartphone on Thursday--targeting business executives--which comes outfitted with the Hermes Agent. This agent can purportedly handle schedules and tasks on a user's behalf and "connect to enterprise systems."

Large-scale Protein Language Models (PLMs) have improved performance in protein prediction tasks, ranging from 3D structure prediction to various function predictions. In particular, AlphaFold, a ground-breaking AI system, could potentially reshape structural biology. However, the utility of the PLM module in AlphaFold, Evoformer, has not been explored beyond structure prediction. In this paper, we investigate the representation ability of three popular PLMs: ESM-1b (single sequence), MSA-Transformer (multiple sequence alignment), and Evoformer (structural), with a special focus on Evoformer. Specifically, we aim to answer the following key questions: (1) Does the Evoformer trained as part of AlphaFold produce representations amenable to predicting protein function?

In 2017, fresh off a PhD on theoretical chemistry, John Jumper heard rumors that Google DeepMind had moved on from game-playing AI to a secret project to predict the structures of proteins. He applied for a job. Just three years later, Jumper and CEO Demis Hassabis had led the development of an AI system called AlphaFold 2 that was able to predict the structures of proteins to within the width of an atom, matching lab-level accuracy, and doing it many times faster--returning results in hours instead of months. Last year, Jumper and Hassabis shared a Nobel Prize in chemistry. Now that the hype has died down, what impact has AlphaFold really had? How are scientists using it?

In 2017, fresh off a PhD on theoretical chemistry, John Jumper heard rumors that Google DeepMind had moved on from building AI that played games with superhuman skill and was starting up a secret project to predict the structures of proteins. He applied for a job. Just three years later, Jumper celebrated a stunning win that few had seen coming. With CEO Demis Hassabis, he had co-led the development of an AI system called AlphaFold 2 that was able to predict the structures of proteins to within the width of an atom, matching the accuracy of painstaking techniques used in the lab, and doing it many times faster--returning results in hours instead of months. AlphaFold 2 had cracked a 50-year-old grand challenge in biology.

The acceleration of artificial intelligence (AI) in science is recognized and many scholars have begun to explore its role in interdisciplinary collaboration. However, the mechanisms and extent of this impact are still unclear. This study, using AlphaFold's impact on structural biologists, examines how AI technologies influence interdisciplinary collaborative patterns. By analyzing 1,247 AlphaFold-related papers and 7,700 authors from Scopus, we employ bibliometric analysis and causal inference to compare interdisciplinary collaboration between AlphaFold adopters and non-adopters. Contrary to the widespread belief that AI facilitates interdisciplinary collaboration, our findings show that AlphaFold increased structural biology-computer science collaborations by just 0.48%, with no measurable effect on other disciplines. Specifically, AI creates interdisciplinary collaboration demands with specific disciplines due to its technical characteristics, but this demand is weakened by technological democratization and other factors. These findings demonstrate that artificial intelligence (AI) alone has limited efficacy in bridging disciplinary divides or fostering meaningful interdisciplinary collaboration.

Recent advances in protein structure prediction, such as AlphaFold, have demonstrated the power of deep neural architectures like the Evoformer for capturing complex spatial and evolutionary constraints on protein conformation. However, the depth of the Evoformer, comprising 48 stacked blocks, introduces high computational costs and rigid layerwise discretization. Inspired by Neural Ordinary Differential Equations (Neural ODEs), we propose a continuous-depth formulation of the Evoformer, replacing its 48 discrete blocks with a Neural ODE parameterization that preserves its core attention-based operations. This continuous-time Evoformer achieves constant memory cost (in depth) via the adjoint method, while allowing a principled trade-off between runtime and accuracy through adaptive ODE solvers. Benchmarking on protein structure prediction tasks, we find that the Neural ODE-based Evoformer produces structurally plausible predictions and reliably captures certain secondary structure elements, such as alpha-helices, though it does not fully replicate the accuracy of the original architecture. However, our model achieves this performance using dramatically fewer resources, just 17.5 hours of training on a single GPU, highlighting the promise of continuous-depth models as a lightweight and interpretable alternative for biomolecular modeling. This work opens new directions for efficient and adaptive protein structure prediction frameworks.

Abstract--Computational protein design is experiencing a transformation driven by AI/ML. However, the range of potential protein sequences and structures is astronomically vast, even for moderately sized proteins. Hence, achieving convergence between generated and predicted structures demands substantial computational resources for sampling. The Integrated Machine-learning for Protein Structures at Scale (IMPRESS) offers methods and advanced computing systems for coupling AI to high-performance computing tasks, enabling the ability to evaluate the effectiveness of protein designs as they are developed, as well as the models and simulations used to generate data and train models. This paper introduces IMPRESS and demonstrates the development and implementation of an adaptive protein design protocol and its supporting computing infrastructure. This leads to increased consistency in the quality of protein design and enhanced throughput of protein design due to dynamic resource allocation and asynchronous workload execution.

AlphaFold, Evoformer, has not been explored beyond structure prediction.

Simulators have revolutionized scientific practice across the natural sciences. By generating data that reliably approximate real-world phenomena, they enable scientists to accelerate hypothesis testing and optimize experimental designs [1, 2]. This is perhaps best illustrated by AlphaFold, a Nobel-prize winning simulator in chemistry that predicts protein structures from amino acid sequences, enabling rapid prototyping of molecular interactions, drug targets, and protein functions [1]. In the behavioral sciences, a reliable participant simulator--a system capable of producing human-like behavior across cognitive tasks--would represent a similarly transformative advance [3]. Recently, Binz et al. introduced Centaur, a large language model (LLM) fine-tuned on human data from 160 experiments, proposing its use not only as a model of cognition but also as a participant simulator for "in silico prototyping of experimental studies" [4], e.g., to advance automated cognitive science [3, 5]. Although Centaur demonstrates strong predictive accuracy, its generative behavior-- a critical criterion for a participant simulator--systematically diverges from human data. This suggests that, while Centaur is a significant step toward predicting human behavior, it does not yet meet the standards of a reliable participant simulator or an accurate model of cognition. A core criterion for any behavioral simulator is its ability to generate behavioral patterns observed in experiments.