Oberli, Matthias A., Tamborrini, Marco, Tsai, Yu-Hsuan ![]() |
Official URL: http://dx.doi.org/10.1021/ja104027w
Abstract
The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Chemistry |
Subjects: | Q Science > QD Chemistry |
Publisher: | American Chemical Society |
ISSN: | 0002-7863 |
Last Modified: | 04 Mar 2023 02:45 |
URI: | https://orca.cardiff.ac.uk/id/eprint/73728 |
Citation Data
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