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Biology subjects

Pak, M. A.

Publications and source records attributed to Pak, M. A..

4 recordsLinked to original sources

Bento: Benchmarking Classical and AI Docking on Drug Design-Relevant Data

AO_SCPLOWBSTRACTC_SCPLOWRecent advances in artificial intelligence have introduced deep learning and co-folding approaches for predicting protein-ligand complexes, raising the question of their applicability and how they compare with classical docking methods. In this work, we present a thorough benchmarking study of eleven tools for protein-ligand interaction prediction, spanning classical molecular docking methods, deep learning-based models, and co-folding algorithms. While most related benchmarking efforts primarily assess the generalization capacity, we extend the analysis to also evaluate the performance on drug design-relevant data and across different classes of protein-ligand complexes. Here, we introduce BO_SCPLOWENTOC_SCPLOW, a comprehensive benchmark that evaluates 11 tools for protein-ligand interaction prediction - both established and recently developed - across four test datasets and multiple derived subsets in a pocket-aware setup. We show that 1) careful dataset curation is essential - filtering by pocket structural similarity and controlling ligand complexity exposes generalization failures that are obscured in conventional benchmarks; 2) classical and deep learning-based docking tools perform similarly well on drug-like ligands, making them comparably useful for virtual screening, with physics-based methods offering a clear advantage in speed; 3) co-folding tools outperform other approaches on structurally complex ligands, whereas most methods achieve similar accuracy on regular small molecules; and 4) all methods struggle to generalize to unseen pockets, with deep learning models being the most prone to overfitting. Overall, our results show that while current docking and DL-based approaches are reliable for many drug-design-relevant scenarios, genuine pocket-level generalization remains an open challenge. BO_SCPLOWENTOC_SCPLOW provides a rigorous and transparent framework for diagnosing these limitations and guiding the development of more robust protein-ligand prediction models. The data and code of Bento are available at https://github.com/LigandPro/Bento.

bioinformatics↗

The new mega dataset combined with a deep neural network makes progress in predicting the impact of single mutations on protein stability

Prediction of proteins stability change ({Delta}{Delta}G) due to single mutation is important for biotechnology, medicine, and our understanding of physics underlying protein folding. Despite the recent tremendous success in 3D protein structure prediction, the apparently simpler problem of predicting the effect of mutations on protein stability has been hampered by the low amount of experimental data. With the recent high-throughput measurements of mutational effects in mega experiment for ~850,000 mutations [Tsuboyama et al., bioRxiv, 2022] it becomes possible to apply the state-of-the-art deep learning methods. Here we explore the ability of ESM2 deep neural network architecture with added Light Attention mechanism to predict the change of protein stability due to single mutations. The resulting method ABYSSAL predicts well the data from the mega experiment (Pearson correlation 0.85) while the prediction of {Delta}{Delta}G values from previous experiments is more modest (Pearson correlation 0.50). ABYSSAL also shows a perfect satisfaction of the antisymmetry property. The ABYSSAL training demonstrated that the dataset should contain around ~100,000 data points for taking advantage of the state-of-the-art deep learning methods. Overall, our study shows great perspectives for developing the deep learning {Delta}{Delta}G predictors.

bioinformatics↗

Using AlphaFold to predict the impact of single mutations on protein stability and function

AlphaFold changed the field of structural biology by achieving three-dimensional (3D) structure prediction from protein sequence at experimental quality. The astounding success even led to claims that the protein folding problem is "solved". However, protein folding problem is more than just structure prediction from sequence. Presently, it is unknown if the AlphaFold-triggered revolution could help to solve other problems related to protein folding. Here we assay the ability of AlphaFold to predict the impact of single mutations on protein stability ({Delta}{Delta}G) and function. To study the question we extracted metrics from AlphaFold predictions before and after single mutation in a protein and correlated the predicted change with the experimentally known {Delta}{Delta}G values. Additionally, we correlated the AlphaFold predictions on the impact of a single mutation on structure with a large scale dataset of single mutations in GFP with the experimentally assayed levels of fluorescence. We found a very weak or no correlation between AlphaFold output metrics and change of protein stability or fluorescence. Our results imply that AlphaFold cannot be immediately applied to other problems or applications in protein folding.

bioinformatics↗

Best templates outperform homology models in predicting the impact of mutations on protein stability

MotivationPrediction of protein stability change upon mutation ({Delta}{Delta}G) is crucial for facilitating protein engineering and understanding of protein folding principles. Robust prediction of protein folding free energy change requires the knowledge of protein three-dimensional (3D) structure. Unfortunately, protein 3D structure is not always available. In this case, one can still predict the protein stability change by constructing a homology model of the protein; however, the accuracy of homology model-based {Delta}{Delta}G predictions is unknown. The perspectives of using 3D structures of the best templates are also unclear. ResultsTo investigate these questions, we used the most popular and accurate publicly available tools: FoldX for stability change prediction and I-Tasser for homology modeling. We found that both homology models and best templates worsen the {Delta}{Delta}G prediction, with best templates performing 1.5 times better than homology models. For AlphaFold models, we also found that the best templates seem to outperform protein models. Our findings imply using the 3D structures of the best templates for {Delta}{Delta}G prediction if the 3D protein structure is unavailable. Contactd.ivankov@skoltech.ru

bioinformatics↗