WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy.
We report a novel method to detect angular conformational changes of a molecular motor in a manner sensitive enough to achieve acquisition rates with a time resolution of 2.5mus (equivalent to 400,000fps). We show that this method has sufficient sensitivity to resolve the velocity of the F(1)-ATPase...
मुख्य लेखकों: | , , , , |
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स्वरूप: | Journal article |
भाषा: | English |
प्रकाशित: |
2008
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_version_ | 1826292708548804608 |
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author | Spetzler, D York, J Martin, J Ishmukhametov, R Frasch, W |
author_facet | Spetzler, D York, J Martin, J Ishmukhametov, R Frasch, W |
author_sort | Spetzler, D |
collection | OXFORD |
description | We report a novel method to detect angular conformational changes of a molecular motor in a manner sensitive enough to achieve acquisition rates with a time resolution of 2.5mus (equivalent to 400,000fps). We show that this method has sufficient sensitivity to resolve the velocity of the F(1)-ATPase gamma-subunit as it travels from one conformational state to another (transition time). Rotation is detected via a gold nanorod attached to the rotating gamma-subunit of an immobilized F(1)-ATPase. Variations in scattered light intensity allow precise measurement of changes in angular position of the rod below the diffraction limit of light. |
first_indexed | 2024-03-07T03:18:52Z |
format | Journal article |
id | oxford-uuid:b6be96ec-d6d9-4dd5-b09f-dca3a862b28b |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:18:52Z |
publishDate | 2008 |
record_format | dspace |
spelling | oxford-uuid:b6be96ec-d6d9-4dd5-b09f-dca3a862b28b2022-03-27T04:43:13ZWITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b6be96ec-d6d9-4dd5-b09f-dca3a862b28bEnglishSymplectic Elements at Oxford2008Spetzler, DYork, JMartin, JIshmukhametov, RFrasch, WWe report a novel method to detect angular conformational changes of a molecular motor in a manner sensitive enough to achieve acquisition rates with a time resolution of 2.5mus (equivalent to 400,000fps). We show that this method has sufficient sensitivity to resolve the velocity of the F(1)-ATPase gamma-subunit as it travels from one conformational state to another (transition time). Rotation is detected via a gold nanorod attached to the rotating gamma-subunit of an immobilized F(1)-ATPase. Variations in scattered light intensity allow precise measurement of changes in angular position of the rod below the diffraction limit of light. |
spellingShingle | Spetzler, D York, J Martin, J Ishmukhametov, R Frasch, W WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title | WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title_full | WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title_fullStr | WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title_full_unstemmed | WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title_short | WITHDRAWN: Microsecond resolution of enzymatic conformational changes using dark-field microscopy. |
title_sort | withdrawn microsecond resolution of enzymatic conformational changes using dark field microscopy |
work_keys_str_mv | AT spetzlerd withdrawnmicrosecondresolutionofenzymaticconformationalchangesusingdarkfieldmicroscopy AT yorkj withdrawnmicrosecondresolutionofenzymaticconformationalchangesusingdarkfieldmicroscopy AT martinj withdrawnmicrosecondresolutionofenzymaticconformationalchangesusingdarkfieldmicroscopy AT ishmukhametovr withdrawnmicrosecondresolutionofenzymaticconformationalchangesusingdarkfieldmicroscopy AT fraschw withdrawnmicrosecondresolutionofenzymaticconformationalchangesusingdarkfieldmicroscopy |