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Better together: building protein oligomers naturally and by design

Protein oligomers are more common in nature than monomers, with dimers being the most prevalent final structural state observed in known structures. From a biological perspective, this makes sense as it conserves vital molecular resources that may be wasted simply by generating larger single polypep...

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Detalles Bibliográficos
Autores principales: Gwyther, Rebecca E.A., Jones, D. Dafydd, Worthy, Harley L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925524/
https://www.ncbi.nlm.nih.gov/pubmed/31803901
http://dx.doi.org/10.1042/BST20190283
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author Gwyther, Rebecca E.A.
Jones, D. Dafydd
Worthy, Harley L.
author_facet Gwyther, Rebecca E.A.
Jones, D. Dafydd
Worthy, Harley L.
author_sort Gwyther, Rebecca E.A.
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description Protein oligomers are more common in nature than monomers, with dimers being the most prevalent final structural state observed in known structures. From a biological perspective, this makes sense as it conserves vital molecular resources that may be wasted simply by generating larger single polypeptide units, and allows new features such as cooperativity to emerge. Taking inspiration from nature, protein designers and engineers are now building artificial oligomeric complexes using a variety of approaches to generate new and useful supramolecular protein structures. Oligomerisation is thus offering a new approach to sample structure and function space not accessible through simply tinkering with monomeric proteins.
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spelling pubmed-69255242020-01-02 Better together: building protein oligomers naturally and by design Gwyther, Rebecca E.A. Jones, D. Dafydd Worthy, Harley L. Biochem Soc Trans Review Articles Protein oligomers are more common in nature than monomers, with dimers being the most prevalent final structural state observed in known structures. From a biological perspective, this makes sense as it conserves vital molecular resources that may be wasted simply by generating larger single polypeptide units, and allows new features such as cooperativity to emerge. Taking inspiration from nature, protein designers and engineers are now building artificial oligomeric complexes using a variety of approaches to generate new and useful supramolecular protein structures. Oligomerisation is thus offering a new approach to sample structure and function space not accessible through simply tinkering with monomeric proteins. Portland Press Ltd. 2019-12-20 2019-12-05 /pmc/articles/PMC6925524/ /pubmed/31803901 http://dx.doi.org/10.1042/BST20190283 Text en © 2019 The Author(s) https://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review Articles
Gwyther, Rebecca E.A.
Jones, D. Dafydd
Worthy, Harley L.
Better together: building protein oligomers naturally and by design
title Better together: building protein oligomers naturally and by design
title_full Better together: building protein oligomers naturally and by design
title_fullStr Better together: building protein oligomers naturally and by design
title_full_unstemmed Better together: building protein oligomers naturally and by design
title_short Better together: building protein oligomers naturally and by design
title_sort better together: building protein oligomers naturally and by design
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6925524/
https://www.ncbi.nlm.nih.gov/pubmed/31803901
http://dx.doi.org/10.1042/BST20190283
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