Anand Kumar Srivastava

The paper introduces SOP-Multi-π, a coarse-grained model with rescaled aromatic interactions to better simulate IDPs and their phase behavior in condensates.

This study shows that phosphoinositide protonation microstates determine AKT1 membrane binding specificity and how mutations alter this interaction.

Morpheus-3D detects and localizes fold-switching proteins using sequence-based entropy profiles, outperforming existing methods and revealing widespread structural plasticity across proteomes.

This study uses thermodynamic analysis to uncover the molecular driving forces behind temperature-induced fold-switching in a designed metamorphic protein, providing a statistical thermodynamic framework for future protein engineering.

This study shows that calcitonin activates the Hippo pathway via CTR to inhibit YAP/TAZ in glioblastoma, with structural defects in CTR mutants impairing this effect.

This paper uses multiscale modeling to investigate how SNX1-SNX5 heterodimers recognize cargo and membranes in a retromer-independent manner.

This study reveals how palmitoylation of PSD95 reorients its domains to promote membrane association and clustering, with lipid composition modulating this process.

The paper introduces a machine learning method to unambiguously identify kinked beta sheets in protein structures and demonstrates its application in analyzing prion-like proteins.

This paper uses simulations to show that highly ordered lipid bilayers exhibit glass-like dynamics with soft fluid channels, which may facilitate molecular interactions.

This study identifies SIRT2 as a regulator of global protein synthesis by modulating Rheb-GTPase activity, showing its potential as a therapeutic target for diseases with increased protein synthesis.

Morpheus predicts fold-switching proteins by analyzing structural fragments across proteomes, identifying 10% of proteins with metamorphic behavior.

This paper computationally designs peptide inhibitors targeting α-Synuclein monomers, fibrils, and liquid condensates using multiscale modeling to reduce aggregation and modulate conformational dynamics.

The paper introduces SOP-MULTI, a coarse-grained force field for simulating multi-domain and intrinsically disordered proteins, validated against experimental scattering data.

This study demonstrates that the REHT method efficiently samples membrane-bound conformations of the Osh4 ALPS peptide, revealing a preference for horizontal over vertical conformations.