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Biology subjects

Dass, R.

Publications and source records attributed to Dass, R..

2 recordsLinked to original sources

Interpretable Machine Learning Decodes Soil Microbiome's Response to Drought Stress

BackgroundExtreme weather events induced by climate change, particularly droughts, have detrimental consequences for crop yields and food security. Concurrently, these conditions provoke substantial changes in the soil metagenome and affect plant health. Early recognition of soil affected by drought enables farmers to implement appropriate agricultural management practices. In this context, interpretable Machine Learning holds immense potential for drought stress classification in the soil metagenome based on marker taxa. ResultsThis study demonstrates that the metagenomic approach of Differential Abundance Analysis methods and Machine Learning-based Shapley Additive Explanation values provide similar information. They exhibit their potential as complementary approaches for identifying marker taxa and investigating their enrichment or depletion under drought stress in grass lineages. Additionally, the Random Forest Classifier trained on a diverse range of relative abundance data from the soil metagenome of various plant species achieves a high accuracy of 92.3 % at the genus rank for drought stress prediction. It demonstrates its generalization capacity for the lineages tested. ConclusionsIn the detection of drought stress in the soil metagenome, this study emphasizes the potential of an optimized and generalized location-based ML classifier. By identifying marker taxa, this approach holds promising implications for microbe-assisted plant breeding programs and contributes to the development of sustainable agriculture practices. These findings are crucial for preserving global food security in the face of climate change.

bioinformatics↗

The contribution of electrostatics to hydrogen exchange in the unfolded protein state

Although electrostatics have long been recognized to play an important role in hydrogen exchange (HX) with solvent, the quantitative assessment of its magnitude in the unfolded state has hitherto been lacking. This limits the utility of HX as a quantitative method to study protein stability, folding and dynamics. Using the intrinsically disordered human protein -synuclein as a proxy for the unfolded state, we show that a hybrid mean-field approach can effectively compute the electrostatic potential at all backbone amide positions along the chain. From the electrochemical potential a fourfold reduction in hydroxide concentration near the protein backbone is predicted for the C-terminal domain, a prognosis that is in direct agreement with experimentally-derived protection factors from NMR spectroscopy. Thus, impeded HX for the C-terminal region of -synuclein is not the result of intramolecular hydrogen bonding and/or structure formation.

biophysics↗