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相关论文: Reconstructing the free energy landscape of a mech…

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The equilibrium free energy landscape of off-lattice model heteropolymers as a function of an internal coordinate, namely the end-to-end distance, is reconstructed from out-of-equilibrium steered molecular dynamics data. This task is…

统计力学 · 物理学 2008-09-17 Stefano Luccioli , Alberto Imparato , Alessandro Torcini

Equilibrium and out-of-equilibrium transitions of an off-lattice protein model have been identified and studied. In particular, the out-of-equilibrium dynamics of the protein undergoing mechanical unfolding is investigated, and by using a…

软凝聚态物质 · 物理学 2010-07-14 A. Imparato , S. Luccioli , A. Torcini

A simple lattice model, recently introduced as a generalization of the Wako--Sait\^o model of protein folding, is used to investigate the properties of widely studied molecules under external forces. The equilibrium properties of the model…

软凝聚态物质 · 物理学 2007-10-16 A. Imparato , A. Pelizzola , M. Zamparo

We used the atomic force microscope to manipulate and unfold individual molecules of the titin I27 domain and reconstructed its free energy surface using Jarzynski's equality. The free energy surface for both stretching and unfolding was…

生物物理 · 物理学 2009-11-13 Nolan C. Harris , Yang Song , Ching-Hwa Kiang

The Jarzynski identity can be applied to instances when a microscopic system is pulled repeatedly but quickly along some coordinate, allowing the calculation of an equilibrium free energy profile along the pulling coordinate from a set of…

统计力学 · 物理学 2015-06-11 Daun Jeong , Ioan Andricioaei

The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is investigated by using atomic force microscopy. Exploiting a fluctuation relation, the equilibrium free energy as a function of the molecule elongation is…

软凝聚态物质 · 物理学 2008-05-29 A. Imparato , F. Sbrana , M. Vassalli

Structural fluctuations in the thermal equilibrium of the kinesin motor domain are studied using a lattice protein model with Go interactions. By means of the multi-self-overlap ensemble (MSOE) Monte Carlo method and the principal component…

生物大分子 · 定量生物学 2007-06-04 Hiroo Kenzaki , Macoto Kikuchi

A theoretical framework is developed to study the dynamics of protein folding. The key insight is that the search for the native protein conformation is influenced by the rate r at which external parameters, such as temperature, chemical…

生物大分子 · 定量生物学 2009-11-13 Gregg Lois , Jerzy Blawzdziewicz , Corey S. O'Hern

Single molecule pulling experiments provide information about interactions in biomolecules that cannot be obtained by any other method. However, the reconstruction of the molecule's free energy profile from the experimental data is still a…

软凝聚态物质 · 物理学 2009-11-10 Oliver Braun , Andreas Hanke , Udo Seifert

The mechanical unfolding of proteins is investigated by extending the Wako-Saito-Munoz-Eaton model, a simplified protein model with binary degrees of freedom, which has proved successful in describing the kinetics of protein folding. Such a…

软凝聚态物质 · 物理学 2007-05-23 A. Imparato , A. Pelizzola , M. Zamparo

Single molecule force spectroscopy provide details of the underlying energy surfaces of proteins which are essential to the understanding of their unfolding process. Recently, it has been observed experimentally that by pulling proteins in…

统计力学 · 物理学 2009-11-13 R. Rajesh , D. Giri , I. Jensen , S. Kumar

Energetic correlations due to polymeric constraints and the locality of interactions, in conjunction with the apriori specification of the existence of a particularly low energy state, provides a method of introducing the aspect of minimal…

凝聚态物理 · 物理学 2009-10-28 Steven S. Plotkin , Jin Wang , Peter G. Wolynes

We use a free energy functional theory to elucidate general properties of heterogeneously ordering, fast folding proteins, and we test our conclusions with lattice simulations. We find that both structural and energetic heterogeneity can…

无序系统与神经网络 · 物理学 2009-10-31 Steven S. Plotkin , Jose N. Onuchic

A general theoretical framework is developed using free energy functional methods to understand the effects of heterogeneity in the folding of a well-designed protein. Native energetic heterogeneity arising from non-uniformity in native…

无序系统与神经网络 · 物理学 2007-05-23 Steven S. Plotkin , Jose N. Onuchic

The understanding, and even the description of protein folding is impeded by the complexity of the process. Much of this complexity can be described and understood by taking a statistical approach to the energetics of protein conformation,…

chem-ph · 物理学 2008-02-03 J. D. Bryngelson , J. N. Onuchic , N. D. Socci , P. G. Wolynes

Metadynamics is a powerful computational tool to obtain the free energy landscape of complex systems. The Monte Carlo algorithm has proven useful to calculate thermodynamic quantities associated with simplified models of proteins, and thus…

统计力学 · 物理学 2007-10-04 F. Marini , C. Camilloni , D. Provasi , R. A. Broglia , G. Tiana

We review the background, theory and general equations for the analysis of equilibrium protein unfolding experiments, focusing on denaturant and heat-induced unfolding. The primary focus is on the thermodynamics of reversible…

生物物理 · 物理学 2020-12-23 Kresten Lindorff-Larsen , Kaare Teilum

Folding kinetics of a lattice model of protein is studied. It uses the Random Energy Model for the intrachain couplings and a temperature dependent free energy of solvation derived from a realistic hydration model of apolar solutes. The…

统计力学 · 物理学 2008-11-06 Olivier Collet

We study the geometric properties of the energy landscape of coarse-grained, off-lattice models of polymers by endowing the configuration space with a suitable metric, depending on the potential energy function, such that the dynamical…

统计力学 · 物理学 2007-05-23 Lorenzo N. Mazzoni , Lapo Casetti

A fluctuation relation, which is an extended form of the Jarzynski equality, is introduced and discussed. We show how to apply this relation in order to evaluate the free energy landscape of simple systems. These systems are manipulated by…

统计力学 · 物理学 2007-05-23 A. Imparato , L. Peliti
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