INO
CNR
vai_a_storia   vai_a_organizzazione   vai_a_sedi   vai_a_personale   Area Riservata
    English English Version  
 
 

Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke

  Articoli su Riviste JCR/ISI  (anno 2012)

Autori:  Capitanio M., Canepari M., Maffei M., Beneventi D., Monico C., Vanzi F., Bottinelli R., Pavone FS

Affiliazione Autori:  Univ Florence, European Lab Nonlinear Spect, Sesto Fiorentino, Italy; Univ Florence, Dept Phys & Astron, Sesto Fiorentino, Italy; Univ Pavia, Dept Mol Med, I-27100 Pavia, Italy; Univ Florence, Dept Evolutionary Biol, Florence, Italy; Sci Inst Pavia, Fdn Salvatore Maugeri, Pavia, Italy; CNR, Natl Opt Inst, Florence, Italy; Int Ctr Computat Neurophoton, Sesto Fiorentino, Italy

Riassunto:  We describe a dual-trap force-clamp configuration that applies constant loads between a binding protein and an intermittently interacting biological polymer. The method has a measurement delay of only similar to 10 mu s, allows detection of interactions as brief as similar to 100 mu s and probes sub-nanometer conformational changes with a time resolution of tens of microseconds. We tested our method on molecular motors and DNDNA-binding proteins. We could apply constant loads to a single motor domain of myosin before its working stroke was initiated (0.2-1 ms), thus directly measuring its load dependence. We found that, depending on the applied load, myosin weakly interacted (<1 ms) with actin without production of movement, fully developed its working stroke or prematurely detached (<5 ms), thus reducing the working stroke size with load. Our technique extends single-molecule force-clamp spectroscopy and opens new avenues for investigating the effects of forces on biological processes.

Rivista/Giornale:  NATURE METHODS
Volume n.:  9 (10)      Pagine da: 1013  a: 1019
Ulteriori informazioni:  Publisher: NATURE PUBLISHING GROUP, MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND DOI: 10.1038/NMETH.2152
DOI: 10.1038/NMETH.2152

*Impact Factor della Rivista: (2012) 23.565   *Citazioni: 71
data tratti da "WEB OF SCIENCE" (marchio registrato di Thomson Reuters) ed aggiornati a:  19/05/2019

Riferimenti visionabili in IsiWeb of Knowledge: (solo per sottoscrittori)
Per visualizzare la scheda dell'articolo su IsiWeb: Clicca qui
Per visualizzare la scheda delle Citazioni dell'articolo su IsiWeb: Clicca qui

INO © Istituto Nazionale di Ottica - Largo Fermi 6, 50125 Firenze | Tel. 05523081 Fax 0552337755 - P.IVA 02118311006     P.E.C.    Info