http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9922

Beta-connectin studies by small-angle x-ray scattering and single-molecule force spectroscopy by atomic force microscopy (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

Beta-connectin studies by small-angle x-ray scattering and single-molecule force spectroscopy by atomic force microscopy (Articolo in rivista) (literal)

Anno

2011-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1103/PhysRevE.83.051919 (literal)

Alternative label

S. Marchetti (1); F. Sbrana (2); A. Toscano (3); E. Fratini (4); M. Carlà (1); M. Vassalli (2); B. Tiribilli (5); A. Pacini (3); C. M. C. Gambi (1) (2011)
Beta-connectin studies by small-angle x-ray scattering and single-molecule force spectroscopy by atomic force microscopy
in Physical review. E, Statistical, nonlinear, and soft matter physics (Print); American Physical Society (APS), College Pk (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

S. Marchetti (1); F. Sbrana (2); A. Toscano (3); E. Fratini (4); M. Carlà (1); M. Vassalli (2); B. Tiribilli (5); A. Pacini (3); C. M. C. Gambi (1) (literal)

Pagina inizio

051919 (literal)

Pagina fine

051919 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

http://link.aps.org/doi/10.1103/PhysRevE.83.051919 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

83 (literal)

Rivista

Physical review. E, Statistical, nonlinear, and soft matter physics (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

9 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

5 (literal)

Note

ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

1 Department of Physics, University of Florence and CNISM Via G. Sansone 1, IT-50019, Sesto Fiorentino (Florence), Italy 2 Biophysics Institute of the National Research Council, Via De Marini 6, Genova, Italy 3 Department of Anatomy, Histology, and Forensic Medicine, University of Florence, Florence, Italy 4 Department of Chemistry and Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase (CSGI), University of Florence, Via della Lastruccia 3, IT-50019, Sesto Fiorentino (Florence), Italy 5 Complex System Institute of the National Research Council (ISC-CNR), Sesto Fiorentino (Florence), Italy (literal)

Titolo

Beta-connectin studies by small-angle x-ray scattering and single-molecule force spectroscopy by atomic force microscopy (literal)

Abstract

The three-dimensional structure and the mechanical properties of a beta-connectin fragment from human cardiac muscle, belonging to the I band, from I_{27} to I_{34}, were investigated by small-angle x-ray scattering (SAXS) and single-molecule force spectroscopy (SMFS). This molecule presents an entropic elasticity behavior, associated to globular domain unfolding, that has been widely studied in the last 10 years. In addition, atomic force microscopy based SMFS experiments suggest that this molecule has an additional elastic regime, for low forces, probably associated to tertiary structure remodeling. From a structural point of view, this behavior is a mark of the fact that the eight domains in the I_{27}-I_{34} fragment are not independent and they organize in solution, assuming a well-defined three-dimensional structure. This hypothesis has been confirmed by SAXS scattering, both on a diluted and a concentrated sample. Two different models were used to fit the SAXS curves: one assuming a globular shape and one corresponding to an elongated conformation, both coupled with a Coulomb repulsion potential to take into account the protein-protein interaction. Due to the predominance of the structure factor, the effective shape of the protein in solution could not be clearly disclosed. By performing SMFS by atomic force microscopy, mechanical unfolding properties were investigated. Typical sawtooth profiles were obtained and the rupture force of each unfolding domain was estimated. By fitting a wormlike chain model to each peak of the sawtooth profile, the entropic elasticity of octamer was described (literal)

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