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Biomedical subjects

Mona Singh

Publications and source records attributed to Mona Singh.

3 recordsLinked to original sources

Fast, accurate construction of multiple sequence alignments from protein language embeddings.

Multiple sequence alignment (MSA) is a foundational task in computational biology, underpinning protein structure prediction, evolutionary analysis, and domain annotation. Traditional MSA algorithms rely on pairwise amino acid substitution matrices derived from conserved protein families. While effective for aligning closely related sequences, these scoring schemes struggle in the low-identity "twilight zone." Here, we present a new approach for constructing MSAs leveraging amino acid embeddings generated by protein language models (PLMs), which capture rich evolutionary and contextual information from massive and diverse sequence datasets. We introduce a windowed reciprocal-weighted embedding similarity metric that is surprisingly effective in identifying corresponding amino acids across sequences. Building on this metric, we develop ARIES (Alignment via RecIprocal Embedding Similarity), an algorithm that constructs a PLM-generated template embedding and aligns each sequence to this template via dynamic time warping in order to build a global MSA. Across diverse benchmark datasets, ARIES achieves higher accuracies than existing state-of-the-art approaches, especially in low-identity regimes where traditional methods degrade, while scaling almost linearly with the number of sequences to be aligned. Together, these results provide the first large-scale demonstration of the power of PLMs for accurate and scalable MSA construction across protein families of varying sizes and levels of similarity, highlighting the potential of PLMs to transform comparative sequence analysis.

Deep Learning

Locality-aware pooling enhances protein language model performance across varied applications.

MOTIVATION: Protein language models (PLMs) are amongst the most exciting recent advances for characterizing protein sequences, and have enabled a diverse set of applications, including structure determination, functional property prediction, and mutation impact assessment, all from single protein sequences alone. State-of-the-art PLMs leverage transformer architectures originally developed for natural language processing, and are pre-trained on large protein databases to generate contextualized representations of individual amino acids. To harness the power of these PLMs to predict protein-level properties, these per-residue embeddings are typically "pooled" to fixed-size vectors that are further utilized in downstream prediction networks. Common pooling strategies include Cls-Pooling and Avg-Pooling, but neither of these approaches can capture the local substructures and long-range interactions observed in proteins. RESULTS: We propose the use of attention pooling, which can naturally capture these important features of proteins. To make the expensive attention operator (quadratic in the length of the input protein) feasible in practice, we introduce bag-of-mer pooling, or BoM-Pooling, a locality-aware hierarchical pooling technique that combines windowed average pooling with attention pooling. We empirically demonstrate that both full attention pooling and BoM-Pooling outperform previous pooling strategies on three important, diverse tasks: (i) predicting the activities of two proteins as they are varied; (ii) detecting remote homologs; and (iii) predicting signaling protein interactions with peptides. Overall, our work highlights the advantages of biologically inspired pooling techniques in protein sequence modeling and is a step toward more effective adaptations of language models in biological settings. AVAILABILITY AND IMPLEMENTATION: https://github.com/Singh-Lab/bom-pooling.

Natural Language Processing

KINAID: an orthology-based kinase-substrate prediction and analysis tool for phosphoproteomics.

SUMMARY: Proteome-wide datasets of phosphorylated peptides, either measured in a condition of interest or in response to perturbations, are increasingly becoming available for model organisms across the evolutionary spectrum. We introduce KINAID (KINase Activity and Inference Dashboard), an interactive and extensible tool written in Dash/Plotly, that predicts kinase-substrate interactions, uncovers and displays kinases whose substrates are enriched amongst phosphorylated peptides, interactively illustrates kinase-substrate interactions, and clusters phosphopeptides targeted by similar kinases. KINAID is the first tool of its kind that can analyze data from not only Homo sapiens but also 10 additional model organisms (including Mus musculus, Danio rerio, Drosophila melanogaster, Caenorhabditis elegans, and Saccharomyces cerevisiae). We demonstrate KINAID's utility by applying it to recently published S. cerevisiae phosphoproteomics data. AVAILABILITY AND IMPLEMENTATION: Webserver is available at https://kinaid.princeton.edu; open-source python library is available at https://github.com/Singh-Lab/kinaid; archive is available at https://doi.org/10.24433/CO.8460107.v1.

Proteomics