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Literature DB >> 8139653

Single myosin molecule mechanics: piconewton forces and nanometre steps.

Abstract

A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament. Discrete stepwise movements averaging 11 nm were seen under conditions of low load, and single force transients averaging 3-4 pN were measured under isometric conditions. The magnitudes of the single forces and displacements are consistent with predictions of the conventional swinging-crossbridge model of muscle contraction.

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Year: 1994 PMID： 8139653 DOI： 10.1038/368113a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

491 in total

1. Imaging of thermal activation of actomyosin motors.

Authors: H Kato; T Nishizaka; T Iga; K Kinosita; S Ishiwata
Journal: Proc Natl Acad Sci U S A Date: 1999-08-17 Impact factor: 11.205

2. Continuous detection of extracellular ATP on living cells by using atomic force microscopy.

Authors: S W Schneider; M E Egan; B P Jena; W B Guggino; H Oberleithner; J P Geibel
Journal: Proc Natl Acad Sci U S A Date: 1999-10-12 Impact factor: 11.205

3. In vitro motility speed of slow myosin extracted from single soleus fibres from young and old rats.

Authors: P Höök; X Li; J Sleep; S Hughes; L Larsson
Journal: J Physiol Date: 1999-10-15 Impact factor: 5.182

4. Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.

Authors: K A Palmiter; M J Tyska; D E Dupuis; N R Alpert; D M Warshaw
Journal: J Physiol Date: 1999-09-15 Impact factor: 5.182

Single myosin molecule mechanics: piconewton forces and nanometre steps.

1. Imaging of thermal activation of actomyosin motors.

2. Continuous detection of extracellular ATP on living cells by using atomic force microscopy.

3. In vitro motility speed of slow myosin extracted from single soleus fibres from young and old rats.

4. Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.

5. Detection of fluorescently labeled actin-bound cross-bridges in actively contracting myofibrils.

6. Processive movement of single 22S dynein molecules occurs only at low ATP concentrations.

7. The mechanochemistry of molecular motors.

8. Temperature change does not affect force between single actin filaments and HMM from rabbit muscles.

9. Comparative single-molecule and ensemble myosin enzymology: sulfoindocyanine ATP and ADP derivatives.

Review 10. Searching for kinesin's mechanical amplifier.