D. D. Prakashchand

This paper investigates how a short synthetic β-peptide forms transmembrane pores in lipid bilayers through molecular dynamics simulations, showing sequence-dependent pore formation and membrane disruption.

This paper uses molecular dynamics simulations to show that phospholipid binding induces conformational changes in apoE3, leading to an open structure that may facilitate receptor recognition.

The paper identifies non-affine displacements as key to resolving the free energy landscape of macromolecules using time-structured independent component analysis and Markov state models.

The paper identifies collective displacements in apo-proteins that correlate with binding pathways without requiring actual binding events.