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Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
A new method is described for measuring motions of protein domains in their native environment on the physiological timescale. Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a reconsti...
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| Published in: | Nature (London) 1999-07, Vol.400 (6743), p.425-430 |
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| Main Authors: | , , , , , , , , , , , |
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| cites | cdi_FETCH-LOGICAL-c458t-7b55ff0ce19a0c9f2a30c798d58fae2f4fbe3528a8fa2987d7d54bebf0834d913 |
| container_end_page | 430 |
| container_issue | 6743 |
| container_start_page | 425 |
| container_title | Nature (London) |
| container_volume | 400 |
| creator | Corrie, J. E. T. Brandmeier, B. D. Ferguson, R. E. Trentham, D. R. Kendrick-Jones, J. Hopkins, S. C. Heide, U. A. van der Goldman, Y. E. Sabido-David, C. Dale, R. E. Criddle, S. Irving, M. |
| description | A new method is described for measuring motions of protein domains in their native environment on the physiological timescale. Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a reconstituted macromolecular complex is determined by combining fluorescence polarization data from a small number of such labelled cysteine pairs. This approach bridges the gap between
in vitro
studies of protein structure and cellular studies of protein function and is used here to measure the tilt and twist of the myosin light-chain domain with respect to actin filaments in single muscle cells. The results reveal the structural basis for the lever-arm action of the light-chain domain of the myosin motor during force generation in muscle. |
| doi_str_mv | 10.1038/22704 |
| format | article |
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in vitro
studies of protein structure and cellular studies of protein function and is used here to measure the tilt and twist of the myosin light-chain domain with respect to actin filaments in single muscle cells. The results reveal the structural basis for the lever-arm action of the light-chain domain of the myosin motor during force generation in muscle.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/22704</identifier><identifier>PMID: 10440371</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cellular biology ; Chickens ; Contractile proteins ; Cross-Linking Reagents ; Cysteine - chemistry ; Escherichia coli ; Fluorescence Polarization ; Fundamental and applied biological sciences. Psychology ; Holoproteins ; Humanities and Social Sciences ; Light ; Models, Molecular ; multidisciplinary ; Muscle Contraction ; Muscle, Skeletal - chemistry ; Muscle, Skeletal - physiology ; Muscular system ; Myosin Light Chains - chemistry ; Myosin Light Chains - physiology ; Physiology ; Protein Conformation ; Proteins ; Rabbits ; Recombinant Proteins - chemistry ; Rhodamines ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 1999-07, Vol.400 (6743), p.425-430</ispartof><rights>Macmillan Magazines Ltd. 1999</rights><rights>1999 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Jul 29, 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-7b55ff0ce19a0c9f2a30c798d58fae2f4fbe3528a8fa2987d7d54bebf0834d913</citedby><cites>FETCH-LOGICAL-c458t-7b55ff0ce19a0c9f2a30c798d58fae2f4fbe3528a8fa2987d7d54bebf0834d913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1901203$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10440371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Corrie, J. E. T.</creatorcontrib><creatorcontrib>Brandmeier, B. D.</creatorcontrib><creatorcontrib>Ferguson, R. E.</creatorcontrib><creatorcontrib>Trentham, D. R.</creatorcontrib><creatorcontrib>Kendrick-Jones, J.</creatorcontrib><creatorcontrib>Hopkins, S. C.</creatorcontrib><creatorcontrib>Heide, U. A. van der</creatorcontrib><creatorcontrib>Goldman, Y. E.</creatorcontrib><creatorcontrib>Sabido-David, C.</creatorcontrib><creatorcontrib>Dale, R. E.</creatorcontrib><creatorcontrib>Criddle, S.</creatorcontrib><creatorcontrib>Irving, M.</creatorcontrib><title>Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>A new method is described for measuring motions of protein domains in their native environment on the physiological timescale. Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a reconstituted macromolecular complex is determined by combining fluorescence polarization data from a small number of such labelled cysteine pairs. This approach bridges the gap between
in vitro
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Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a reconstituted macromolecular complex is determined by combining fluorescence polarization data from a small number of such labelled cysteine pairs. This approach bridges the gap between
in vitro
studies of protein structure and cellular studies of protein function and is used here to measure the tilt and twist of the myosin light-chain domain with respect to actin filaments in single muscle cells. The results reveal the structural basis for the lever-arm action of the light-chain domain of the myosin motor during force generation in muscle.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>10440371</pmid><doi>10.1038/22704</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1999-07, Vol.400 (6743), p.425-430 |
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| language | eng |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cellular biology Chickens Contractile proteins Cross-Linking Reagents Cysteine - chemistry Escherichia coli Fluorescence Polarization Fundamental and applied biological sciences. Psychology Holoproteins Humanities and Social Sciences Light Models, Molecular multidisciplinary Muscle Contraction Muscle, Skeletal - chemistry Muscle, Skeletal - physiology Muscular system Myosin Light Chains - chemistry Myosin Light Chains - physiology Physiology Protein Conformation Proteins Rabbits Recombinant Proteins - chemistry Rhodamines Science Science (multidisciplinary) |
| title | Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction |
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