Titre :

Rate-dependent force–extension models for single-molecule force spectroscopy experiments

Auteur(s) :

Benedito, Manon [Auteur]
Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Manca, Fabio [Auteur]
Adhésion et Inflammation [LAI]
Centre Interdisciplinaire de Nanoscience de Marseille [CINaM]
Palla, Pier Luca [Auteur]
Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Physique - IEMN [PHYSIQUE - IEMN]
Giordano, Stefano [Auteur]
Institut d’Électronique, de Microélectronique et de Nanotechnologie - UMR 8520 [IEMN]
Acoustique Impulsionnelle & Magnéto-Acoustique Non linéaire - Fluides, Interfaces Liquides & Micro-Systèmes - IEMN [AIMAN-FILMS - IEMN]

Titre de la revue :

Physical Biology

Pagination :

056002

Éditeur :

Institute of Physics: Hybrid Open Access

Date de publication :

2020-09-01

ISSN :

1478-3967

Mot(s)-clé(s) en anglais :

single molecule force spectroscopy
chain of bistable units
spin variables approach
rate-dependent theory

Discipline(s) HAL :

Physique [physics]
Science non linéaire [physics]
Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Single-molecule force spectroscopy (SMFS) techniques allow for the measurements of several static and dynamic features of macromolecules of biological origin. In particular, the atomic force microscopy (AFM), used with a ...
Lire la suite >Single-molecule force spectroscopy (SMFS) techniques allow for the measurements of several static and dynamic features of macromolecules of biological origin. In particular, the atomic force microscopy (AFM), used with a variable pulling rate, provides valuable information on the folding/unfolding dynamics of proteins. We propose here two different models able to describe the out-of-equilibrium statistical mechanics of a chain composed of bistable units. These latter represent the protein domains, which can be either folded or unfolded. Both models are based on the Langevin approach and their implementation allows for investigating the effect of the pulling rate and of the device intrinsic elasticity on the chain unfolding response. The theoretical results (both analytical and numerical) have been compared with experimental data concerning the unfolding of the titin and filamin proteins, eventually obtaining a good agreement over a large range of the pulling rates.Lire moins >

Langue :

Anglais

Vulgarisation :

Non

Collections :

• Institut d'Électronique, de Microélectronique et de Nanotechnologie (IEMN) - UMR 8520

Source :

Harvested from HAL