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Updated: Apr 22, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
Published on: October 15, 2018
Mechanical unfolding of a simple model protein goes beyond the reach of one-dimensional descriptions
R Tapia-Rojo1, S Arregui1, J J Mazo2
1Instituto de Biocomputación y Física de Sistemas Complejos and Departamento de Física de la Materia Condensada, Universidad de Zaragoza, 50009 Zaragoza, Spain.
Abstract:
We study the mechanical unfolding of a simple model protein. The Langevin dynamics results are analyzed using Markov-model methods which allow to describe completely the configurational space of the system. Using transition-path theory we also provide a quantitative description of the unfolding pathways followed by the system. Our study shows a complex dynamical scenario. In particular, we see that the usual one-dimensional picture: free-energy vs end-to-end distance representation, gives a misleading description of the process. Unfolding can occur following different pathways and configurations which seem to play a central role in one-dimensional pictures are not the intermediate states of the unfolding dynamics.
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