Search bioRxiv⌕ Search

Biology subjects

Chen, L. T.

Publications and source records attributed to Chen, L. T..

2 recordsLinked to original sources

PG-LLM: Benchmarking General-Purpose Language Models for Protein Variant Ranking

General-purpose frontier language models are being increasingly utilized for protein-design work, yet their ability to understand and evaluate variant effects remains unclear. Here, we introduce PG-LLM, a benchmark comprising 276 protein-variant prioritization tasks: 217 from ProteinGym and a temporally held-out set of 59 from recently published studies. Each task follows the same format: a language model is asked to rank a list of variant sequences given only the wild-type protein sequence and an assay description with no access to tools, multiple-sequence alignments, or protein structures. We evaluate thirteen language models and 95 published protein predictors on the same variants with the same evaluation metric. Claude Opus 5 (Max) and GPT 5.6 Sol (Max) are the best performing LLMs with Spearman correlations of{rho} = 0.406 and 0.402 respectively. Opus 5 outperforms 49 of 95 published protein predictors, including 41 of 46 sequence-only methods, and approaches ESM2-650M at{rho} = 0.411, but remains below the leading predictor VenusREM at{rho} = 0.523. We observe that variant-ranking performance scales with test-time compute across GPT, Claude, and Gemini models, but gains taper before closing the gap to specialist protein predictors. To address contamination risk, we create a held-out evaluation set with 59 DMS assays from 19 studies whose scores first became public after January 2026. On this set, we observe performance and test time compute scaling trends similar to those on the 217 tasks derived from ProteinGym. PG-LLM shows that tool-free language models capture substantial protein-variant signal, outperforming many sequence-based predictors while remaining below the strongest specialized models.

bioinformatics↗

DPAC: Prediction and Design of Protein-DNA Interactions via Sequence-Based Contrastive Learning

Interactions between DNA and proteins are pivotal in natural biological processes, and designing proteins that can bind to DNA with high specificity is crucial for advancing genomic technologies. Existing state-of-the-art models for both modeling and designing protein-DNA interactions primarily rely on structural information, facing limitations in scalability and efficiency for large-scale applications. Notable methods like AlphaFold 3 and RosettaTTAFold All-Atom exist, but they are inefficient and inherently struggle at modeling conformationally unstable proteins, such as transcription factors, which arguably represent the most important class of DNA-binding proteins. Here, we present DPAC1 (DNA-Protein binding Alignment via Contrastive learning), which leverages pre-trained protein and DNA language models via a contrastive loss to align the two modalities in a high-dimensional shared latent space. DPAC not only significantly accelerates the design process compared to current structure-based methods but also demonstrates a strong ability to differentiate real binders from non-binders. Our model achieves an AUC score of 0.591 on a low identity set, outperforming state-of-the-art structure-based methods. Additionally, DPAC integrates simulated annealing for the design of new protein sequences with optimized DNA binding affinity, successfully recovering binding affinity in engineered sequences by up to 20% in in silico tests. Our results highlight DPACs potential for facilitating the design and discovery of sequence-specific DNA-binding proteins, paving the way for advancements in genomic research and biotechnology applications.

bioengineering↗