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Related papers: Force-Dependent Folding Kinetics of Single Molecul…

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We investigated frictional effects on the folding rates of a human telomerase hairpin (hTR HP) and H-type pseudoknot from the Beet Western Yellow Virus (BWYV PK) using simulations of the Three Interaction Site (TIS) model for RNA. The heat…

Biomolecules · Quantitative Biology 2018-09-18 Naoto Hori , Natalia A. Denesyuk , D. Thirumalai

Non-coding RNA sequences play a great role in controlling a number of cellular functions, thus raising the need to understand their complex conformational dynamics in quantitative detail. In this perspective, we first show that single…

Biomolecules · Quantitative Biology 2012-11-29 Jong-Chin Lin , Changbong Hyeon , D. Thirumalai

Developing accurate and efficient coarse-grained representations of proteins is crucial for understanding their folding, function, and interactions over extended timescales. Our methodology involves simulating proteins with molecular…

Biomolecules · Quantitative Biology 2023-10-11 Carles Navarro , Maciej Majewski , Gianni de Fabritiis

Simple two-state folding kinetics of many small single-domain proteins are characterized by chevron plots with linear folding and unfolding arms consistent with a two-state description of equilibrium thermodynamics. This phenomenon is…

Soft Condensed Matter · Physics 2007-05-23 Huseyin Kaya , Hue Sun Chan

In typical single-molecule force spectroscopy experiments the mechanical unfolding of molecular complexes or biomolecules is studied applying a force ramp to one end of the system while the other end is kept fixed in space. The…

Soft Condensed Matter · Physics 2026-05-18 Marco Oestereich , Jürgen Gauss , Gregor Diezemann

This paper aims at a comprehensive understanding on the novel elastic property of double-stranded DNA (dsDNA) discovered very recently through single-molecule manipulation techniques. A general elastic model for double-stranded biopolymers…

Soft Condensed Matter · Physics 2009-10-31 Haijun Zhou , Yang Zhang , Zhong-can Ou-Yang

Single-molecule atomic force spectroscopy probes elastic properties of titin, ubiquitin and other relevant proteins. We explain bioprotein folding dynamics under both length- and force-clamp by modeling polyprotein modules as particles in a…

Statistical Mechanics · Physics 2016-11-17 L. L. Bonilla , A. Carpio , A. Prados

The process of protein folding from an unfolded state to a biologically active, folded conformation is governed by many parameters e.g the sequence of amino acids, intermolecular interactions, the solvent, temperature and chaperon…

Soft Condensed Matter · Physics 2010-10-19 Pragya Shukla

Kinetics of folding of a protein held in a force-clamp are compared to an unconstrained folding. The comparison is made within a simple topology-based dynamical model of ubiquitin. We demonstrate that the experimentally observed variations…

Biomolecules · Quantitative Biology 2009-11-13 Marek Cieplak , Piotr Szymczak

We describe a systematic approach to construct coarse-grained Markov state models from molecular dynamics data of systems driven into a non-equilibrium steady state. We apply this method to study the globule-stretch transition of a single…

Soft Condensed Matter · Physics 2017-02-28 Fabian Knoch , Thomas Speck

We theoretically investigate the extractable work in single molecule unfolding-folding experiments with applied feedback. Using a simple two-state model, we obtain a description of the full work distribution, from discrete to continuous…

We consider a simple model for the unfolding of RNA tertiary structure under dynamic loading. The opening of such a structure is regarded as a two step process, each corresponding to the overcoming of a single energy barrier. The resulting…

Biomolecules · Quantitative Biology 2009-11-10 Alberto Imparato , Luca Peliti

We present a maximum-caliber method for inferring transition rates of a Markov State Model (MSM) with perturbed equilibrium populations, given estimates of state populations and rates for an unperturbed MSM. It is similar in spirit to…

Biomolecules · Quantitative Biology 2016-05-26 Vincent A. Voelz , Guangfeng Zhou , Hongbin Wan

The mechanical unfolding of a simple RNA hairpin and of a 236--bases portion of the Tetrahymena thermophila ribozyme is studied by means of an Ising--like model. Phase diagrams and free energy landscapes are computed exactly and suggest a…

Soft Condensed Matter · Physics 2009-11-05 A. Imparato , A. Pelizzola , M. Zamparo

In recent years, single molecule force techniques have opened a new avenue to decipher the folding landscapes of biopolymers by allowing us to watch and manipulate the dynamics of individual proteins and nucleic acids. In single molecule…

Biomolecules · Quantitative Biology 2016-11-25 Changbong Hyeon

We review theoretical approaches, experiments and numerical simulations that have been recently proposed to investigate the folding problem in single-domain proteins. From a theoretical point of view, we emphasize the energy landscape…

Biological Physics · Physics 2008-10-20 Ivan Junier , Felix Ritort

Self-positioned nanomembranes such as rolled-up tubes and wrinkled thin films have been potential systems for a variety of applications and basic studies on elastic properties of nanometer-thick systems. Although there is a clear driving…

Mesoscale and Nanoscale Physics · Physics 2014-07-23 Peter Cendula , Angelo Malachias , Christoph Deneke , Suwit Kiravittaya , Oliver G. Schmidt

We introduce a model of thermalized conformations in space of RNA -or single stranded DNA- molecules, which includes the possibility of hairpin formation. This model contains the usual secondary structure information, but extends it to the…

Soft Condensed Matter · Physics 2007-05-23 Andrea Montanari , Marc Mezard

To what extent do general features of folding/unfolding kinetics of small globular proteins follow from their thermodynamic properties? To address this question, we investigate a new simplifed protein chain model that embodies a cooperative…

Soft Condensed Matter · Physics 2007-05-23 Huseyin Kaya , Hue Sun Chan

The determination of the folding mechanisms of proteins is critical to understand the topological change that can propagate Alzheimer and Creutzfeld-Jakobs diseases, among others. The computational community has paid considerable attention…

Biomolecules · Quantitative Biology 2007-05-23 Guanghong Wei , Normand Mousseau , Philippe Derreumaux