Imperial College London

ProfessorSteveMarston

Faculty of MedicineNational Heart & Lung Institute

Emeritus Professor
 
 
 
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Contact

 

+44 (0)20 7594 2732s.marston Website

 
 
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Location

 

433ICTEM buildingHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Holohan:2005:10.1049/ip-nbt:20045003,
author = {Holohan, S-JP and Marston, SB},
doi = {10.1049/ip-nbt:20045003},
journal = {IEE Proc Nanobiotechnol},
pages = {113--120},
title = {Force-velocity relationship of single actin filament interacting with immobilised myosin measured by electromagnetic technique.},
url = {http://dx.doi.org/10.1049/ip-nbt:20045003},
volume = {152},
year = {2005}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The effect of applying an external load to actin filaments moving in the in vitro motility assay is studied. Bead-tailed actin filaments were made by polymerising actin onto 2.8 microm diameter Dynabeads conjugated with gelsolin-G actin. These were introduced into a motility cell coated with 100 microg/ml rabbit fast skeletal myosin in the presence of ATP and 0.5% methylcellulose. The motility cell was inserted between the pole-pieces of an electromagnet and the fluorescent beads and filaments were observed. The force-current relationship of the electromagnet was determined from the velocity of free beads in viscous solution and Stokes' equation. The magnet produced up to 6 pN force on the Dynabeads at 1 A. Many bead-tailed actin filaments stuck to the surface, but the beads that did move moved at the same speed as unloaded f-actin in the same cell. Bead-tailed filaments slowed down under an increasing magnetic load, eventually stalled and then slid backward under increasing load before detaching from the surface. Single-filament force-velocity curves were constructed and a stalling force of about 0.6 pN/mm of actin filament estimated.
AU - Holohan,S-JP
AU - Marston,SB
DO - 10.1049/ip-nbt:20045003
EP - 120
PY - 2005///
SN - 1478-1581
SP - 113
TI - Force-velocity relationship of single actin filament interacting with immobilised myosin measured by electromagnetic technique.
T2 - IEE Proc Nanobiotechnol
UR - http://dx.doi.org/10.1049/ip-nbt:20045003
UR - https://www.ncbi.nlm.nih.gov/pubmed/16441167
VL - 152
ER -