MOTIVATION: Data scarcity limits the characterization of protein fitness landscapes and the development of accurate variant effect prediction models. To address this challenge, we introduce fitness translocation, a data augmentation strategy that generates synthetic variants for a target protein by leveraging variant fitness data previously measured in homologous proteins. Using embeddings from protein language models, the method computes the difference between each homolog variant and its wild type and applies these offsets to the target wild-type embedding to create synthetic variants in embedding space. RESULTS: We illustrate the utility of fitness translocation in the context of variant effect prediction on three protein families: IGPS, GFP, and SARS-CoV-2 spike proteins, across different models and training data sizes. Fitness translocation consistently improves predictive performance, particularly under limited training data, and is effective even when augmenting with remote homologs sharing as little as 35% sequence identity. These results illustrate how biologically grounded data augmentation can expand and diversify protein fitness landscapes, supporting more data-efficient protein engineering. AVAILABILITY AND IMPLEMENTATION: The code and datasets are available at https://github.com/adrienmialland/ProtFitTrans.

In this paper, we propose a system of bidirectional power routing for inter-house multi-energy management systems that utilize electricity and hydrogen as energy carriers. The key is to share private facilities such as photovoltaic panels and batteries among a group of houses along with a common hydrogen system. A power router of line switching type is introduced as a physical interface to realize the sharing economy between households. The proposed system offers a unique measure to address the urgent challenges of today’s multi-energy system, namely increasing the renewables’ self-consumption, enhancing the energy system’s resilience, and providing traceability of hydrogen in terms of renewability certification. We also present an experimental demonstration under a simplified scenario using prototype hardware.

Accurate variant effect prediction has broad impacts on protein engineering. Recent machine learning approaches toward this end are based on representation learning, by which feature vectors are learned and generated from unlabeled sequences. However, it is unclear how to effectively learn evolutionary properties of an engineering target protein from homologous sequences, taking into account the protein's sequence-level structure called domain architecture (DA). Additionally, no optimal protocols are established for incorporating such properties into Transformer, the neural network well-known to perform the best in natural language processing research. This article proposes DA-aware evolutionary fine-tuning, or 'evotuning', protocols for Transformer-based variant effect prediction, considering various combinations of homology search, fine-tuning and sequence vectorization strategies. We exhaustively evaluated our protocols on diverse proteins with different functions and DAs. The results indicated that our protocols achieved significantly better performances than previous DA-unaware ones. The visualizations of attention maps suggested that the structural information was incorporated by evotuning without direct supervision, possibly leading to better prediction accuracy.

When this paper originally published, it was erroneously published alongside supplementary data from another paper. This has now been corrected online, and the correct supplementary data has been published. The publisher apologises for this error.