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Biology subjects

Bardhan, K.

Publications and source records attributed to Bardhan, K..

3 recordsLinked to original sources

Deep-Interact Studio: An Interactive Deep Learning Model Building Platform for Biomolecular Interaction Prediction

MotivationDeep learning has rapidly become essential for predicting biomolecular interactions; however, most web-tools expose only a single, pre-built model with a fixed, non-configurable architecture that users cannot redesign, retrain on their own data, or compare; they are typically dedicated to one interaction type and often one species, and report prediction scores with little interpretability. These constraints force researchers across several disconnected, single-purpose tools and limit the flexibility, reproducibility, and long-term usability of existing platforms. ResultsWe present Deep-Interact Studio, a unified, web-based deep-learning platform that addresses these limitations by shifting interaction prediction from a model-centric to a user-driven, comparative, and interpretable paradigm. Within a single interface spanning all four interaction classes, namely protein-protein, drugtarget, RNA-protein, and protein-DNA, users design their own model architectures layer by layer, configure training hyperparameters, and train them on their own data, including custom, species-specific datasets. Multiple user-built models can then be trained under identical conditions and compared side by side at both the training and inference levels, while integrated interpretability, including SHAP-based feature attribution, embedding-space visualization, and interaction hub analysis, turns predictions into auditable, mechanistically grounded results. Deep-Interact Studio is, to our knowledge, the only such platform to combine fine-grained per-layer model customization with multi-model comparison and interpretability, offering a flexible and transparent alternative to fixed, single-purpose tools. Availability and implementationDeep-Interact Studio is freely available as a web application at https://deepinteract.compbiosysnbu.in/, with no login or installation required.

bioinformatics↗

Functional insights into a peculiar tetra-modular LPMO from the human pathogen Enterobacter cloacae

Enterobacter cloacae is a Gram-negative nosocomial human pathogen that inhabits diverse ecological niches. Its genome encodes a conserved set of putative chitin-active enzymes, including a peculiar lytic polysaccharide monooxygenase (LPMO), termed EcLPMO, which we functionally characterized in this study. EcLPMO is a tetra-modular protein consisting of an auxiliary activity family 10 (AA10) catalytic domain, two central domains of unknown function (DUF-A and DUF-B), and a C-terminal carbohydrate-binding module (CBM73). Functional assays using full-length EcLPMO and its truncated variants demonstrated that the AA10 domain oxidatively cleaves chitin at the C1 position. The CBM73 module enhances chitin binding and promotes synergy with endogenous chitinases. Notably, EcLPMO displayed a particularly strong synergistic effect with the unimodular chitinase EcChiA, leading to up to 14-fold and 60-fold increases in GlcNAc release from - and {beta}-chitin, respectively. Deletion of both DUFs reduced EcLPMO activity. While DUF-A alone and the association of DUF-A and DUF-B showed limited chitin binding, DUF-B alone exhibited no binding, suggesting a distinct role. Unexpectedly, using state-of-the-art structural modelling (AlphaFold3), we observed that the DUF-B domain contains two highly conserved histidines that coordinate the AA10-bound copper, forming a previously unreported inter-domain tetra-histidine copper coordination center. These findings highlight the structural and functional complexity of EcLPMO and suggest that its accessory domains, particularly DUF-B, may contribute to enzyme stability and substrate interaction. We speculate that DUF-B may protect the LPMO active site from oxidative damage, a feature that could prove crucial in its ecological and pathogenic contexts.

biochemistry↗

Does plant root architecture respond to potassium nutrition under water stress? A case from rice seedling root system architectural and growth responses.

The root is the sensing organ for potassium (K) and water availability. We evaluated whether K availability influences root architecture and contributes to drought tolerance under moisture stress. Rice seedling growth was severely affected by low K availability under water stress, and the substantial reductions in root projected area, maximum width, and width to depth ratio were observed. High K availability helps maintain root top and bottom angles and reduces root steepness under mild water stress, but over K nutrition does not ensure higher seedling growth. Under severe water stress, the steepness was more regulated by water than K availability.

plant biology↗