Probing the Conformational Dynamics of Intrinsically Disordered Proteins via MD Simulations

EasyChair Preprint 12158

Abstract

Intrinsically disordered proteins (IDPs) play pivotal roles in numerous cellular processes, yet their dynamic structural behaviors remain challenging to elucidate using traditional experimental techniques. Molecular dynamics (MD) simulations have emerged as a powerful tool for investigating the conformational dynamics of IDPs at atomic resolution. In this study, we employed MD simulations to explore the conformational landscape of several representative IDPs and to elucidate their structural transitions and interactions with biomolecular partners. Through extensive MD simulations, we observed a wide range of dynamic behaviors in IDPs, including transient secondary structure formation, ensemble averaging of multiple conformations, and interactions with solvent molecules. Our results revealed that the conformational dynamics of IDPs are highly sensitive to environmental factors such as temperature, pH, and the presence of ligands or other interacting proteins. Overall, our findings provide valuable insights into the conformational dynamics of IDPs and highlight the utility of MD simulations in elucidating the complex structural behavior of these biologically important molecules.

Keyphrases: Intrinsically disordered proteins (IDPs), Molecular dynamics (MD) simulations, conformational dynamics

@booklet{EasyChair:12158,
  author    = {Jane Elsa and Halil Neval},
  title     = {Probing the Conformational Dynamics of Intrinsically Disordered Proteins via MD Simulations},
  howpublished = {EasyChair Preprint 12158},
  year      = {EasyChair, 2024}}