Nanometre resolution tracking of myosin-1b motility.
The movement produced by a small number of myosin molecular motors was measured with nanometre precision using single-molecule fluorescence localisation methods. The positional precision of the measurements was sufficient to reveal fluctuations in sliding velocity due to stochastic interactions betw...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2003
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| _version_ | 1797089467190738944 |
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| author | Wallace, M Batters, C Coluccio, L Molloy, J |
| author_facet | Wallace, M Batters, C Coluccio, L Molloy, J |
| author_sort | Wallace, M |
| collection | OXFORD |
| description | The movement produced by a small number of myosin molecular motors was measured with nanometre precision using single-molecule fluorescence localisation methods. The positional precision of the measurements was sufficient to reveal fluctuations in sliding velocity due to stochastic interactions between individual myosin motors and the actin filament. Dependence of sliding velocity upon filament length was measured and fluctuations in velocity were quantified by autocorrelation analysis. Optical tweezers-based nanometry was used to measure the myosin-1b step-size directly. The 10 nm power-stroke and its duty cycle ratio were consistent with values derived from in vitro sliding assays. |
| first_indexed | 2024-03-07T03:04:30Z |
| format | Journal article |
| id | oxford-uuid:b208a758-99a4-44f2-9882-7c951a3cd1b9 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:04:30Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:b208a758-99a4-44f2-9882-7c951a3cd1b92022-03-27T04:08:47ZNanometre resolution tracking of myosin-1b motility.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b208a758-99a4-44f2-9882-7c951a3cd1b9EnglishSymplectic Elements at Oxford2003Wallace, MBatters, CColuccio, LMolloy, JThe movement produced by a small number of myosin molecular motors was measured with nanometre precision using single-molecule fluorescence localisation methods. The positional precision of the measurements was sufficient to reveal fluctuations in sliding velocity due to stochastic interactions between individual myosin motors and the actin filament. Dependence of sliding velocity upon filament length was measured and fluctuations in velocity were quantified by autocorrelation analysis. Optical tweezers-based nanometry was used to measure the myosin-1b step-size directly. The 10 nm power-stroke and its duty cycle ratio were consistent with values derived from in vitro sliding assays. |
| spellingShingle | Wallace, M Batters, C Coluccio, L Molloy, J Nanometre resolution tracking of myosin-1b motility. |
| title | Nanometre resolution tracking of myosin-1b motility. |
| title_full | Nanometre resolution tracking of myosin-1b motility. |
| title_fullStr | Nanometre resolution tracking of myosin-1b motility. |
| title_full_unstemmed | Nanometre resolution tracking of myosin-1b motility. |
| title_short | Nanometre resolution tracking of myosin-1b motility. |
| title_sort | nanometre resolution tracking of myosin 1b motility |
| work_keys_str_mv | AT wallacem nanometreresolutiontrackingofmyosin1bmotility AT battersc nanometreresolutiontrackingofmyosin1bmotility AT colucciol nanometreresolutiontrackingofmyosin1bmotility AT molloyj nanometreresolutiontrackingofmyosin1bmotility |