Publication | Closed Access
Construction of Protein Nanowires through Cucurbit[8]uril‐based Highly Specific Host–Guest Interactions: An Approach to the Assembly of Functional Proteins
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Citations
21
References
2013
Year
EngineeringProtein AssemblyEnzyme SimulationLipid PeroxidationMolecular BiologyDimeric Glutathione S-transferaseRedox BiologySelf-assembled Protein NanowiresOxidative StressProtein NanowiresBioanalysisFunctional ProteinsProteomicsBiochemistryNanobiotechnologyNanotechnologyBioconjugationBiomolecular EngineeringHost-guest ChemistryNatural SciencesMetalloproteinBiotechnologyProtein Engineering
Getting your proteins in a row: Self-assembled protein nanowires were designed by utilizing highly specific supramolecular interactions of cucurbit[8]uril (CB[8]) and a tripeptide FGG-tag attached on the N-termini of dimeric glutathione S-transferase (GST). With the aid of enzyme simulation, model protein GST was converted into a selenoenzyme glutathione peroxidase mimic, and the CB[8]-induced Se-FGG-GST(Y6C) nanowires demonstrated excellent antioxidative capacity. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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