Literature DB >> 11463650

Quantal sarcomere-length changes in relaxed single myofibrils.

F Blyakhman1, A Tourovskaya, G H Pollack.   

Abstract

We carried out experiments on single isolated myofibrils in which thin filaments had been functionally removed, leaving the connecting (titin) filaments as the sole agent taking up the length change. With technical advances that gave sub-nanometer detectability we examined the time course of single sarcomere-length change when the myofibril was ramp-released or ramp-stretched by a motor. The sarcomere-length change was stepwise. Step sizes followed a consistent pattern: the smallest was approximately 2.3 nm, and others were integer multiples of that value. The approximately 2.3-nm step quantum is the smallest consistent biomechanical event ever demonstrated. Although the length change must involve the connecting filament, the size of the quantum is an order of magnitude smaller than anticipated from folding of Ig- or fibronectin-like domains, implying either that folding occurs in sub-domain units or that other mechanisms are involved.

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Year:  2001        PMID: 11463650      PMCID: PMC1301578          DOI: 10.1016/S0006-3495(01)75766-9

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  14 in total

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  6 in total

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Journal:  J Muscle Res Cell Motil       Date:  2005       Impact factor: 2.698

6.  Stepwise sliding of single actin and Myosin filaments.

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  6 in total

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