Papers
2
Total Citations
85
H-Index
2
About
Romain Iehl is a computational biophysicist whose research focuses on the mechanistic simulation of protein–ligand interactions, with a particular emphasis on the dynamic processes of ligand binding, unbinding, and the associated conformational changes in proteins. His major contributions include the development of innovative computational tools to study these complex molecular events. Notably, he created MoMA-LigPath, a web server that simulates protein–ligand unbinding pathways, helping researchers understand how interactions occurring far from the active site influence molecular specificity and activity. This tool has garnered 46 citations, reflecting its utility in the field. In earlier work, Iehl pioneered a mechanical disassembly method to simulate ligand-induced conformational changes in proteins, addressing a key challenge in computational biology by modeling the internal diffusion of ligands and the resulting structural rearrangements. His 2010 paper on this method has been cited 39 times. Iehl’s work is highly relevant for drug discovery and molecular design, providing researchers with accessible, web-based resources to explore the dynamic nature of biomolecular interactions.
Research Focus
Key Achievements
Top Papers
- 1MoMA-LigPath: a web server to simulate protein–ligand unbinding46 citations · 2013
- 2