Regensburg 2025 – scientific programme

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BP: Fachverband Biologische Physik

BP 32: Computational Biophysics II

BP 32.4: Talk

Friday, March 21, 2025, 10:15–10:30, H46

Helical transition of protein chain: An in silico study — •tika ram bhandari and martin girard — Max Planck Institute for Polymer Research, Mainz, Germany

Structural transformations in biomolecular systems are critical for physiological functions, with folding and unfolding transitions governing numerous cellular activities. Misfolding of proteins, however, is a key factor in the onset of severe diseases, emphasizing the need for comprehensive studies to understand and control these processes. Computational simulations provide valuable insights into such mechanisms. Here, we employed coarse-grained molecular simulations coupled with Hamiltonian Replica Exchange method to investigate the disordered-to-helical transition of IM30, the bacterial counterpart of the ESCRT-III. By systematically varying the strength of hydrogen bonds, we simulated an in-silico denaturation process, enabling a detailed analysis of the structural properties underlying this transition. Furthermore, we explore the impact of point mutations on the protein's helical propensity using free energy calculations. These approaches provide a deeper understanding of the molecular mechanisms influencing folding behavior and highlights the role of specific mutations in modulating protein structure.

Keywords: protein; molecular dynamics; structural transition; free energy