title: Mechanical unfolding of a simple model protein goes beyond the reach of one-dimensional descriptions.
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.
authors.affiliation: Instituto de Biocomputación y Física de Sistemas Complejos and Departamento de Física de la Materia Condensada, Universidad de Zaragoza, 50009 Zaragoza, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Tapia-Rojo
authors.affiliation: Instituto de Biocomputación y Física de Sistemas Complejos and Departamento de Física de la Materia Condensada, Universidad de Zaragoza, 50009 Zaragoza, Spain.
authors.forename: S
authors.initials: S
authors.lastname: Arregui
authors.affiliation: Instituto de Ciencia de Materiales de Aragón and Departamento de Física de la Materia Condensada, CSIC-Universidad de Zaragoza, 50009 Zaragoza, Spain.
authors.forename: J J
authors.initials: JJ
authors.lastname: Mazo
authors.affiliation: Instituto de Biocomputación y Física de Sistemas Complejos and Departamento de Física de la Materia Condensada, Universidad de Zaragoza, 50009 Zaragoza, Spain.
authors.forename: F
authors.initials: F
authors.lastname: Falo
mesh_terms: D008390:Markov Chains; D008958:Models, Molecular; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins