Protein mechanical unfolding: A model with binary variables
نویسندگان
چکیده
منابع مشابه
Protein mechanical unfolding: a model with binary variables.
A simple model, recently introduced as a generalization of the Wako-Saito; model of protein folding, is used to investigate the properties of widely studied molecules under external forces. The equilibrium properties of the model proteins, together with their energy landscape, are studied on the basis of the exact solution of the model. Afterwards, the kinetic response of the molecules to a for...
متن کاملAn Ising-Like model for protein mechanical unfolding
The mechanical unfolding of proteins is investigated by extending the Wako-Saitô-Muñoz-Eaton model, a simplified protein model with binary degrees of freedom, which has proved successful in describing the kinetics of protein folding. Such a model is generalized by including the effect of an external force, and its thermodynamics turns out to be exactly solvable. We consider two molecules, the 2...
متن کاملMechanical unfolding studies of protein molecules
Atomic force microscopy (AFM) enables the pick up of a single protein molecule to apply a mechanical force. This technique, called "force spectroscopy," provides unique information about the intermediates and free energy landscape of the mechanical unfolding of proteins. In this review, we introduce the AFM-based single molecule force spectroscopy of proteins and describe recent studies that an...
متن کاملMechanical and chemical unfolding of a single protein: a comparison.
Is the mechanical unraveling of protein domains by atomic force microscopy (AFM) just a technological feat or a true measurement of their unfolding? By engineering a protein made of tandem repeats of identical Ig modules, we were able to get explicit AFM data on the unfolding rate of a single protein domain that can be accurately extrapolated to zero force. We compare this with chemical unfoldi...
متن کاملMechanical 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 pathways followed by the system. Our study shows a complex dynamical scenario. In particular, we see ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Chemical Physics
سال: 2007
ISSN: 0021-9606,1089-7690
DOI: 10.1063/1.2776271