Mechanical unfolding of a simple model protein goes beyond the reach of one-dimensional descriptions

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 path...

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Veröffentlicht in:	The Journal of chemical physics 2014-10, Vol.141 (13), p.135102-135102
Hauptverfasser:	Tapia-Rojo, R, Arregui, S, Mazo, J J, Falo, F
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Sprache:	eng
Schlagworte:	Markov Chains Models, Molecular Pictures Protein Unfolding Proteins Proteins - chemistry Thermodynamics
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container_title	The Journal of chemical physics
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creator	Tapia-Rojo, R Arregui, S Mazo, J J Falo, F
description	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.
doi_str_mv	10.1063/1.4896620
format	Article
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subjects	Markov Chains Models, Molecular Pictures Protein Unfolding Proteins Proteins - chemistry Thermodynamics
title	Mechanical unfolding of a simple model protein goes beyond the reach of one-dimensional descriptions
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