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  Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles

Mallagaray, A., Rademacher, C., Parra, F., Hansman, G., & Peters, T. (2016). Saturation transfer difference nuclear magnetic resonance titrations reveal complex multistep-binding of l-fucose to norovirus particles. Glycobiology, 27(1), 80-86. doi:10.1093/glycob/cww070.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-2138-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-BF91-C
Genre: Journal Article

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 Creators:
Mallagaray, Alvaro, Author
Rademacher, Christoph1, Author              
Parra, Francisco, Author
Hansman, Grant, Author
Peters, Thomas, Author
Affiliations:
1Christoph Rademacher, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863300              

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 Abstract: Recently, combined nuclear magnetic resonance (NMR), native MS and X-ray crystallographic studies have demonstrated that binding of histo-blood group antigens (HBGAs) to norovirus capsid protein (P-dimers) is a cooperative process involving four binding pockets. Here, we show that binding to norovirus virus-like particles (VLPs) is even more complex. We performed sexually transmitted disease NMR titration experiments with two representative genotypes of norovirus VLPs using l-fucose as a minimal HBGA. Compared to titrations with P-dimers, the corresponding binding isotherms reflect at least six distinct binding events.

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 Dates: 2016-08-032016
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1093/glycob/cww070
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Title: Glycobiology
  Other : Glycobiology
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 27 (1) Sequence Number: - Start / End Page: 80 - 86 Identifier: ISSN: 0959-6658