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Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance
The recognition of carbohydrates by proteins is an important element in many biological events like cell targeting, tumor invasion, immune response or bacterial and viral adhesion to host cells. 1,2 Besides structural data obtained from X-ray crystallography or NMR spectroscopy, the analysis of carb...
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Published in: | Journal of carbohydrate chemistry 2000-01, Vol.19 (8), p.1083-1089 |
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Language: | English |
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cited_by | cdi_FETCH-LOGICAL-c344t-378d8dba31403a4b82f3b771e5b99c70db6360814c8d412347fbc2453ddb9cc33 |
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cites | cdi_FETCH-LOGICAL-c344t-378d8dba31403a4b82f3b771e5b99c70db6360814c8d412347fbc2453ddb9cc33 |
container_end_page | 1089 |
container_issue | 8 |
container_start_page | 1083 |
container_title | Journal of carbohydrate chemistry |
container_volume | 19 |
creator | Weimar, Thomas Haase, Bernd Köhli, Thies |
description | The recognition of carbohydrates by proteins is an important element in many biological events like cell targeting, tumor invasion, immune response or bacterial and viral adhesion to host cells.
1,2
Besides structural data obtained from X-ray crystallography or NMR spectroscopy, the analysis of carbohydrate protein interactions should also take into consideration other biophysical parameters such as dissociation constants or kinetic rate constants of the complex. However, these parameters are often difficult to determine due to the rather low affinity of the systems under investigation. |
doi_str_mv | 10.1080/07328300008544136 |
format | article |
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1,2
Besides structural data obtained from X-ray crystallography or NMR spectroscopy, the analysis of carbohydrate protein interactions should also take into consideration other biophysical parameters such as dissociation constants or kinetic rate constants of the complex. However, these parameters are often difficult to determine due to the rather low affinity of the systems under investigation.</description><identifier>ISSN: 0732-8303</identifier><identifier>EISSN: 1532-2327</identifier><identifier>DOI: 10.1080/07328300008544136</identifier><language>eng</language><publisher>Taylor & Francis Group</publisher><ispartof>Journal of carbohydrate chemistry, 2000-01, Vol.19 (8), p.1083-1089</ispartof><rights>Copyright Taylor & Francis Group, LLC 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c344t-378d8dba31403a4b82f3b771e5b99c70db6360814c8d412347fbc2453ddb9cc33</citedby><cites>FETCH-LOGICAL-c344t-378d8dba31403a4b82f3b771e5b99c70db6360814c8d412347fbc2453ddb9cc33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Weimar, Thomas</creatorcontrib><creatorcontrib>Haase, Bernd</creatorcontrib><creatorcontrib>Köhli, Thies</creatorcontrib><title>Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance</title><title>Journal of carbohydrate chemistry</title><description>The recognition of carbohydrates by proteins is an important element in many biological events like cell targeting, tumor invasion, immune response or bacterial and viral adhesion to host cells.
1,2
Besides structural data obtained from X-ray crystallography or NMR spectroscopy, the analysis of carbohydrate protein interactions should also take into consideration other biophysical parameters such as dissociation constants or kinetic rate constants of the complex. However, these parameters are often difficult to determine due to the rather low affinity of the systems under investigation.</description><issn>0732-8303</issn><issn>1532-2327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkN1KAzEQhYMoWKsP4F1eYDXZyTZb8KaUqoUFRe31kl8a2U0kibT79m6pdwWdmxmY8x0OB6FbSu4oqck94VDWQMapK8YozM7QhFZQFiWU_BxNDv9iFMAlukrpc9SVvKITtGnCDi-sdd7lAS9FlGE76CiywY1R2Xm89tlEMZ7BJ7zai955o_HO5S1-_45WKINfO5H64PGbScELr8w1urCiS-bmd0_R5nH1sXwumpen9XLRFAoYywXwWtdaCqCMgGCyLi1Izqmp5HyuONFyBjNSU6ZqzWgJjFupSlaB1nKuFMAU0aOviiGlaGz7FV0v4tBS0h56aU96GZmHI-O8DbEXuxA73WYxdCHaOKZ3qYW_cP4vfkK1eZ_hB5y5ewc</recordid><startdate>20000101</startdate><enddate>20000101</enddate><creator>Weimar, Thomas</creator><creator>Haase, Bernd</creator><creator>Köhli, Thies</creator><general>Taylor & Francis Group</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20000101</creationdate><title>Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance</title><author>Weimar, Thomas ; Haase, Bernd ; Köhli, Thies</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-378d8dba31403a4b82f3b771e5b99c70db6360814c8d412347fbc2453ddb9cc33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Weimar, Thomas</creatorcontrib><creatorcontrib>Haase, Bernd</creatorcontrib><creatorcontrib>Köhli, Thies</creatorcontrib><collection>CrossRef</collection><jtitle>Journal of carbohydrate chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Weimar, Thomas</au><au>Haase, Bernd</au><au>Köhli, Thies</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance</atitle><jtitle>Journal of carbohydrate chemistry</jtitle><date>2000-01-01</date><risdate>2000</risdate><volume>19</volume><issue>8</issue><spage>1083</spage><epage>1089</epage><pages>1083-1089</pages><issn>0732-8303</issn><eissn>1532-2327</eissn><abstract>The recognition of carbohydrates by proteins is an important element in many biological events like cell targeting, tumor invasion, immune response or bacterial and viral adhesion to host cells.
1,2
Besides structural data obtained from X-ray crystallography or NMR spectroscopy, the analysis of carbohydrate protein interactions should also take into consideration other biophysical parameters such as dissociation constants or kinetic rate constants of the complex. However, these parameters are often difficult to determine due to the rather low affinity of the systems under investigation.</abstract><pub>Taylor & Francis Group</pub><doi>10.1080/07328300008544136</doi><tpages>7</tpages></addata></record> |
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title | Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance |
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