Single‐particle visualization of assembly: I. Dimerization in a planar zone
Summary Single‐particle fluorescence microscopy of association/dissociation is required for analysis of biological assembly reactions. Toward achieving this goal, Wang et al. (J. Microsc., 2004, 213, 101–109) used molten agarose to concentrate thermally diffusing particles in a thin zone of solution...
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Veröffentlicht in: | Journal of microscopy (Oxford) 2005-01, Vol.217 (1), p.83-92 |
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creator | WANG, H. WU, I. YANG, Q. CATALANO, C. E. SERWER, P. |
description | Summary
Single‐particle fluorescence microscopy of association/dissociation is required for analysis of biological assembly reactions. Toward achieving this goal, Wang et al. (J. Microsc., 2004, 213, 101–109) used molten agarose to concentrate thermally diffusing particles in a thin zone of solution next to the surface of a coverglass (plane of concentration). The present study details the first real‐time, single‐particle analysis of the association/dissociation of thermally diffusing particles in the plane of concentration. The test particles were procapsids of bacteriophage λ (radius = 31 nm). Quantification of thermal motion was developed and used to determine whether co‐diffusing particles were bound to each other. The data are explained by (1) the presence of a molten agarose‐generated barrier that is 93–155 nm from the coverglass surface, and (2) non‐random orientation of procapsid dimers in the plane of concentration. |
doi_str_mv | 10.1111/j.0022-2720.2005.01438.x |
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Single‐particle fluorescence microscopy of association/dissociation is required for analysis of biological assembly reactions. Toward achieving this goal, Wang et al. (J. Microsc., 2004, 213, 101–109) used molten agarose to concentrate thermally diffusing particles in a thin zone of solution next to the surface of a coverglass (plane of concentration). The present study details the first real‐time, single‐particle analysis of the association/dissociation of thermally diffusing particles in the plane of concentration. The test particles were procapsids of bacteriophage λ (radius = 31 nm). Quantification of thermal motion was developed and used to determine whether co‐diffusing particles were bound to each other. The data are explained by (1) the presence of a molten agarose‐generated barrier that is 93–155 nm from the coverglass surface, and (2) non‐random orientation of procapsid dimers in the plane of concentration.</description><identifier>ISSN: 0022-2720</identifier><identifier>EISSN: 1365-2818</identifier><identifier>DOI: 10.1111/j.0022-2720.2005.01438.x</identifier><identifier>PMID: 15655066</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Alexa ; association/dissociation ; bacteriophage ; capsid ; confined thermal motion ; Dimerization ; dye ; fluorescence microscopy ; Image Processing, Computer-Assisted - methods ; Microscopy, Fluorescence ; Viral Proteins - chemistry</subject><ispartof>Journal of microscopy (Oxford), 2005-01, Vol.217 (1), p.83-92</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3988-6bace0661851e47d2351de488bfc668d50bf4516c1e729302413d4ff0087c3c93</citedby><cites>FETCH-LOGICAL-c3988-6bace0661851e47d2351de488bfc668d50bf4516c1e729302413d4ff0087c3c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.0022-2720.2005.01438.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.0022-2720.2005.01438.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15655066$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>WANG, H.</creatorcontrib><creatorcontrib>WU, I.</creatorcontrib><creatorcontrib>YANG, Q.</creatorcontrib><creatorcontrib>CATALANO, C. E.</creatorcontrib><creatorcontrib>SERWER, P.</creatorcontrib><title>Single‐particle visualization of assembly: I. Dimerization in a planar zone</title><title>Journal of microscopy (Oxford)</title><addtitle>J Microsc</addtitle><description>Summary
Single‐particle fluorescence microscopy of association/dissociation is required for analysis of biological assembly reactions. Toward achieving this goal, Wang et al. (J. Microsc., 2004, 213, 101–109) used molten agarose to concentrate thermally diffusing particles in a thin zone of solution next to the surface of a coverglass (plane of concentration). The present study details the first real‐time, single‐particle analysis of the association/dissociation of thermally diffusing particles in the plane of concentration. The test particles were procapsids of bacteriophage λ (radius = 31 nm). Quantification of thermal motion was developed and used to determine whether co‐diffusing particles were bound to each other. The data are explained by (1) the presence of a molten agarose‐generated barrier that is 93–155 nm from the coverglass surface, and (2) non‐random orientation of procapsid dimers in the plane of concentration.</description><subject>Alexa</subject><subject>association/dissociation</subject><subject>bacteriophage</subject><subject>capsid</subject><subject>confined thermal motion</subject><subject>Dimerization</subject><subject>dye</subject><subject>fluorescence microscopy</subject><subject>Image Processing, Computer-Assisted - methods</subject><subject>Microscopy, Fluorescence</subject><subject>Viral Proteins - chemistry</subject><issn>0022-2720</issn><issn>1365-2818</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMlOwzAQQC0EoqXwC8gnbgleYsdB4oDKVlTEAThbjuMgV85C3EDbE5_AN_IlJLTAEeYyI82bRQ8AiFGIuziehQgREpCYoJAgxEKEIyrCxRYYYspZQAQW22D4Aw3AnvczhJBgAu2CAWacMcT5ENze2_LJmY-391o1c6udgS_Wt8rZlZrbqoRVDpX3pkjd8gROQnhuC9N8N20JFaydKlUDV1Vp9sFOrpw3B5s8Ao-XFw_j62B6dzUZn00DTRMhAp4qbbrzWDBsojgjlOHMREKkueZcZAylecQw19jEJKGIRJhmUZ53_8ea6oSOwNF6b91Uz63xc1lYr43rPjFV6yWPqUAEiz9BnMQ85jjuQLEGdVN535hc1o0tVLOUGMneuZzJXqfsdcreufxyLhfd6OHmRpsWJvsd3EjugNM18GqdWf57sby5nfQV_QTyS49w</recordid><startdate>200501</startdate><enddate>200501</enddate><creator>WANG, H.</creator><creator>WU, I.</creator><creator>YANG, Q.</creator><creator>CATALANO, C. E.</creator><creator>SERWER, P.</creator><general>Blackwell Science Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>200501</creationdate><title>Single‐particle visualization of assembly: I. Dimerization in a planar zone</title><author>WANG, H. ; WU, I. ; YANG, Q. ; CATALANO, C. E. ; SERWER, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3988-6bace0661851e47d2351de488bfc668d50bf4516c1e729302413d4ff0087c3c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alexa</topic><topic>association/dissociation</topic><topic>bacteriophage</topic><topic>capsid</topic><topic>confined thermal motion</topic><topic>Dimerization</topic><topic>dye</topic><topic>fluorescence microscopy</topic><topic>Image Processing, Computer-Assisted - methods</topic><topic>Microscopy, Fluorescence</topic><topic>Viral Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WANG, H.</creatorcontrib><creatorcontrib>WU, I.</creatorcontrib><creatorcontrib>YANG, Q.</creatorcontrib><creatorcontrib>CATALANO, C. E.</creatorcontrib><creatorcontrib>SERWER, P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of microscopy (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WANG, H.</au><au>WU, I.</au><au>YANG, Q.</au><au>CATALANO, C. E.</au><au>SERWER, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Single‐particle visualization of assembly: I. Dimerization in a planar zone</atitle><jtitle>Journal of microscopy (Oxford)</jtitle><addtitle>J Microsc</addtitle><date>2005-01</date><risdate>2005</risdate><volume>217</volume><issue>1</issue><spage>83</spage><epage>92</epage><pages>83-92</pages><issn>0022-2720</issn><eissn>1365-2818</eissn><abstract>Summary
Single‐particle fluorescence microscopy of association/dissociation is required for analysis of biological assembly reactions. Toward achieving this goal, Wang et al. (J. Microsc., 2004, 213, 101–109) used molten agarose to concentrate thermally diffusing particles in a thin zone of solution next to the surface of a coverglass (plane of concentration). The present study details the first real‐time, single‐particle analysis of the association/dissociation of thermally diffusing particles in the plane of concentration. The test particles were procapsids of bacteriophage λ (radius = 31 nm). Quantification of thermal motion was developed and used to determine whether co‐diffusing particles were bound to each other. The data are explained by (1) the presence of a molten agarose‐generated barrier that is 93–155 nm from the coverglass surface, and (2) non‐random orientation of procapsid dimers in the plane of concentration.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15655066</pmid><doi>10.1111/j.0022-2720.2005.01438.x</doi><tpages>10</tpages></addata></record> |
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subjects | Alexa association/dissociation bacteriophage capsid confined thermal motion Dimerization dye fluorescence microscopy Image Processing, Computer-Assisted - methods Microscopy, Fluorescence Viral Proteins - chemistry |
title | Single‐particle visualization of assembly: I. Dimerization in a planar zone |
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