Publications by authors named "Subinoy Adhikari"
Article Synopsis
- The mis-folding of intrinsically disordered proteins (IDPs) like α-synuclein is linked to neurodegenerative diseases, complicating drug development due to their lack of defined structures.
- A machine learning approach was used to analyze how fasudil, a small molecule, interacts with α-synuclein in water, revealing that fasudil influences the protein's conformational states.
- The findings highlight the significant role of entropic changes in α-synuclein's structure when interacting with small molecules, suggesting this could be key for developing new therapeutic strategies.
Phosphorylation of intrinsically disordered proteins/regions (IDPs/IDRs) has a profound effect in biological functions such as cell signaling, protein folding or unfolding, and long-range allosteric effects. However, here we focus on two IDPs, namely 83-residue IDR transcription factor Ash1 and 92-residue long N-terminal region of CDK inhibitor Sic1 protein, found in , for which experimental measurements of average conformational properties, namely, radius of gyration and structure factor, indicate negligible changes upon phosphorylation. Here, we show that a judicious dissection of conformational ensemble via combination of unsupervised machine learning and extensive molecular dynamics (MD) trajectories can highlight key differences and similarities among the phosphorylated and wild-type IDP.
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