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Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection

The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled‐coils, provide an excellent platform to improve this understanding and to construct novel molecular devices....

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Detalles Bibliográficos
Autores principales: Mueller, Carolin, Grossmann, Tom N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391972/
https://www.ncbi.nlm.nih.gov/pubmed/30411434
http://dx.doi.org/10.1002/anie.201811515
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author Mueller, Carolin
Grossmann, Tom N.
author_facet Mueller, Carolin
Grossmann, Tom N.
author_sort Mueller, Carolin
collection PubMed
description The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled‐coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled‐coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin‐like conformation that opens upon receptor binding. Variation of the coiled‐coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real‐time.
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spelling pubmed-63919722019-03-07 Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection Mueller, Carolin Grossmann, Tom N. Angew Chem Int Ed Engl Communications The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled‐coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled‐coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin‐like conformation that opens upon receptor binding. Variation of the coiled‐coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real‐time. John Wiley and Sons Inc. 2018-11-28 2018-12-21 /pmc/articles/PMC6391972/ /pubmed/30411434 http://dx.doi.org/10.1002/anie.201811515 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Communications
Mueller, Carolin
Grossmann, Tom N.
Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title_full Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title_fullStr Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title_full_unstemmed Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title_short Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
title_sort coiled‐coil peptide beacon: a tunable conformational switch for protein detection
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391972/
https://www.ncbi.nlm.nih.gov/pubmed/30411434
http://dx.doi.org/10.1002/anie.201811515
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