Natural supramolecular protein assemblies
Abstract
Supramolecular protein assemblies are an emerging area within the chemical sciences, which combine the topological structures of the field of supramolecular chemistry and the state-of-the-art chemical biology approaches to unravel the formation and function of protein assemblies. Recent chemical and biological studies on natural multimeric protein structures, including fibers, rings, tubes, catenanes, knots, and cages, have shown that the quaternary structures of proteins are a prerequisite for their highly specific biological functions. In this review, we illustrate that a striking structural diversity of protein assemblies is present in nature. Furthermore, we describe structure–function relationship studies for selected classes of protein architectures, and we highlight the techniques that enable the characterisation of supramolecular protein structures.
Additional Information
© 2015 The Royal Society of Chemistry. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Received 18 Feb 2015, First published online 26 Oct 2015. We thank the Netherlands Research School for Chemical Biology (NRSCB, J. M.), the European Research Council (ERC Advanced Grant, ALPROS-290886, R. J. M. N.) and the Netherlands Organisation for Scientific Research (Rubicon fellowship, M. B. v. E.) for financial support.Attached Files
Published - Natural_supramolecular_protein_assemblies.pdf
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Additional details
- Eprint ID
- 61779
- Resolver ID
- CaltechAUTHORS:20151103-075107447
- Netherlands Research School for Chemical Biology (NRSCB)
- ALPROS-290886
- European Research Council (ERC)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO)
- Created
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2015-11-03Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field