arXiv:2603. 20115v2 Announce Type: replace Abstract: Small protein-family alignments often contain a subset of interest but not enough labeled data to train a conditional generator.
Machine-generated by The Flow from the publisher's headline and feed description — not written or checked by a human. The full article lives at arXiv Machine Learning.
arXiv:2603. 14717v2 Announce Type: replace Abstract: Generating novel protein sequences that respect a family's statistical constraints typically requires training deep generative models on thousands to millions of examples.
arXiv:2605. 16331v2 Announce Type: replace-cross Abstract: Protein language models are increasingly used to guide experimental and clinical decisions, yet it is often unclear whether a confident prediction reflects recognition of biological evidence or retrieval of a statistical default.
FLaG (Frequency‑Domain Latent‑attention Gated Pooling) is a plug‑in token‑aggregation module that transforms encoder outputs into the Fourier domain, summarizes spectral tokens with learnable latent queries, applies a sample‑conditioned channel gate, and reconstructs modulated token representations for downstream pooling. The method is evaluated on antimicrobial peptide activity prediction, CIFAR‑10/100 image classification, and several RoBERTa language tasks, achieving state‑of‑the‑art performance on most metrics. Analyses show that FLaG emphasizes low‑frequency components while selectively amplifying high‑frequency signals in later layers, providing a transferable frequency‑domain bias across protein, visual, and textual representations.
GyroNovo is a new framework for de novo peptide sequencing that improves fragment imputation by guiding the process with decoder errors observed during training. It introduces mass-aware attention using rotary embeddings to encode pairwise mass differences between spectral peaks, and creates easy and hard augmented views of spectra to train the decoder under varying corruption levels. Experiments on NovoBench demonstrate significant gains, with about 9 percentage points higher peptide-level precision and 7 percentage points higher amino-acid-level precision compared to the state-of-the-art baseline.
arXiv:2606. 02629v1 Announce Type: cross Abstract: Protein-protein interactions (PPIs) are essential for many biological processes.
The paper introduces Murmur2Vec, a lightweight, alignment‑free embedding that uses k‑mer counts hashed with MurmurHash to create a compact representation for biological sequences. It provides a full theoretical analysis, including bias/variance formulas, a Johnson–Lindenstrauss‑style concentration bound, and an excess‑risk bound that clarifies the trade‑off between hash‑table size and classifier performance. Empirically, Murmur2Vec matches or surpasses a fine‑tuned 650M‑parameter ESM‑2 protein language model across several classification tasks, including SARS‑CoV‑2 spike lineage and HIV‑1 Env subtype identification.