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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

The thesis examines in detail the folding and unfolding processes of a number of proteins including hbSBD, DDLNF4, single and multi Ubiquitin. Using simplified coarse-grained off-lattice Go model and CD experiments we have shown the…

Biological Physics · Physics 2013-08-13 Maksim Kouza

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

Force-clamp spectroscopy reveals the unfolding and disulfide bond rupture times of single protein molecules as a function of the stretching force, point mutations and solvent conditions. The statistics of these times reveal whether the…

Biological Physics · Physics 2012-12-07 Herbert Lannon , Eric Vanden-Eijnden , Jasna Brujic

The refolding from stretched initial conformations of ubiquitin (PDB ID: 1ubq) under the quenched force is studied using the Go model and the Langevin dynamics. It is shown that the refolding decouples the collapse and folding kinetics. The…

Biomolecules · Quantitative Biology 2009-11-13 Mai Suan Li , Maksim Kouza , Chin-Kun Hu

Mechanically induced protein unfolding in the force-clamp apparatus is shown, in a coarse-grained model of ubiquitin, to have lognormal statistics above a treshold force and exponential below it. Correspondingly, the mean unfolding time is…

Biomolecules · Quantitative Biology 2007-05-23 Piotr Szymczak , Marek Cieplak

We present force-clamp data on the collapse of ubiquitin polyproteins in response to a quench in the force. These nonequilibrium trajectories are analyzed using a general method based on a diffusive assumption of the end-to-end length to…

Biological Physics · Physics 2017-08-23 Herbert Lannon , Eric Vanden-Eijnden , Jasna Brujic

Stretching of a protein by a fluid flow is compared to that in a force-clamp apparatus. The comparison is made within a simple topology-based dynamical model of a protein in which the effects of the flow are implemented using Langevin…

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

Mechanical unfolding and refolding of ubiquitin are studied by Monte Carlo simulations of a Go model with binary variables. The exponential dependence of the time constants on the force is verified, and folding and unfolding lengths are…

Soft Condensed Matter · Physics 2008-04-22 A. Imparato , A. Pelizzola

Recent single-molecule force measurements on single-domain proteins have highlighted a three-state folding mechanism where a stabilized intermediate state (I) is observed on the folding trajectory between the stretched state and the native…

Biological Physics · Physics 2008-10-08 Ivan Junier , Felix Ritort

Biological forces govern essential cellular and molecular processes in all living organisms. Many cellular forces, e.g. those generated in cyclic conformational changes of biological machines, have repetitive components. However, little is…

Biomolecules · Quantitative Biology 2008-09-17 P. Szymczak , Harald Janovjak

We incorporate hydrodynamic interactions in a structure-based model of ubiquitin and demonstrate that the hydrodynamic coupling may reduce the peak force when stretching the protein at constant speed, especially at larger speeds.…

Biomolecules · Quantitative Biology 2015-05-13 P. Szymczak , Marek Cieplak

Most single-molecule studies derive the kinetic rates of native, intermediate, and unfolded states from equilibrium hopping experiments. Here, we apply Kramers kinetic diffusive model to derive the force-dependent kinetic rates of…

Soft Condensed Matter · Physics 2022-04-13 Marc Rico-Pasto , Anna Alemany , Felix Ritort

The mechanical stretching of single poly-proteins is an emerging tool for the study of protein (un)folding, chemical catalysis and polymer physics at the single molecule level. The observed processes i.e unfolding or reduction events, are…

Biomolecules · Quantitative Biology 2014-07-17 Rodolfo I. Hermans

Although known that single domain proteins fold and unfold by parallel pathways, demonstration of this expectation has been difficult to establish in experiments. Unfolding rate, $k_\mathrm{u}(f)$, as a function of force $f$, obtained in…

Soft Condensed Matter · Physics 2016-04-27 Pavel I. Zhuravlev , Michael Hinczewski , Shaon Chakrabarti , Susan Marqusee , D. Thirumalai

Single-molecule experiments with optical tweezers have become an important tool to study the properties and mechanisms of biological systems, such as cells and nucleic acids. In particular, force unzipping experiments have been used to…

Biological Physics · Physics 2019-07-22 Marc Rico-Pasto , Isabel Pastor , Felix Ritort

Repeat proteins are made with tandem copies of similar amino acid stretches that fold into elongated architectures. Due to their symmetry, these proteins constitute excellent model systems to investigate how evolution relates to structure,…

Biomolecules · Quantitative Biology 2022-10-12 Ezequiel A. Galpern , Jacopo Marchi , Thierry Mora , Aleksandra M. Walczak , Diego U. Ferreiro

Cargo distribution within eukaryotic cells relies on the active transport mechanisms driven by molecular motors. Despite their critical role, the intricate relationship between motor transport properties and cargo binding - and its impact…

Biological Physics · Physics 2025-09-09 Amir Shee , Vidur Sabharwal , Sandhya P. Koushika , Amitabha Nandi , Debasish Chaudhuri

Mechanical stretching of secondary structures is studied through molecular dynamics simulations of a Go-like model. Force vs. displacement curves are studied as a function of the stiffness and velocity of the pulling device. The succession…

Soft Condensed Matter · Physics 2007-05-23 Marek Cieplak , Trinh Xuan Hoang , Mark O. Robbins

The dependence of the unfolding pathway of proteins on the pulling speed is investigated. This is done by introducing a simple one-dimensional chain comprising $N$ units, with different characteristic bistable free energies. These units…

Statistical Mechanics · Physics 2016-10-19 C. A. Plata , F. Cecconi , M. Chinappi , A. Prados
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