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Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances
Proteins possess a complex and dynamic structure, which is influenced by external signals and may change as they perform their biological functions. We present an optical approach, distance-encoding photoinduced electron transfer (DEPET), capable of the simultaneous study of protein structure and fu...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6226468/ https://www.ncbi.nlm.nih.gov/pubmed/30413716 http://dx.doi.org/10.1038/s41467-018-07218-6 |
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author | Pantazis, Antonios Westerberg, Karin Althoff, Thorsten Abramson, Jeff Olcese, Riccardo |
author_facet | Pantazis, Antonios Westerberg, Karin Althoff, Thorsten Abramson, Jeff Olcese, Riccardo |
author_sort | Pantazis, Antonios |
collection | PubMed |
description | Proteins possess a complex and dynamic structure, which is influenced by external signals and may change as they perform their biological functions. We present an optical approach, distance-encoding photoinduced electron transfer (DEPET), capable of the simultaneous study of protein structure and function. An alternative to FRET-based methods, DEPET is based on the quenching of small conjugated fluorophores by photoinduced electron transfer: a reaction that requires contact of the excited fluorophore with a suitable electron donor. This property allows DEPET to exhibit exceptional spatial and temporal resolution capabilities in the range pertinent to protein conformational change. We report the first implementation of DEPET on human large-conductance K(+) (BK) channels under voltage clamp. We describe conformational rearrangements underpinning BK channel sensitivity to electrical excitation, in conducting channels expressed in living cells. Finally, we validate DEPET in synthetic peptide length standards, to evaluate its accuracy in measuring sub- and near-nanometer intramolecular distances. |
format | Online Article Text |
id | pubmed-6226468 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-62264682018-11-13 Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances Pantazis, Antonios Westerberg, Karin Althoff, Thorsten Abramson, Jeff Olcese, Riccardo Nat Commun Article Proteins possess a complex and dynamic structure, which is influenced by external signals and may change as they perform their biological functions. We present an optical approach, distance-encoding photoinduced electron transfer (DEPET), capable of the simultaneous study of protein structure and function. An alternative to FRET-based methods, DEPET is based on the quenching of small conjugated fluorophores by photoinduced electron transfer: a reaction that requires contact of the excited fluorophore with a suitable electron donor. This property allows DEPET to exhibit exceptional spatial and temporal resolution capabilities in the range pertinent to protein conformational change. We report the first implementation of DEPET on human large-conductance K(+) (BK) channels under voltage clamp. We describe conformational rearrangements underpinning BK channel sensitivity to electrical excitation, in conducting channels expressed in living cells. Finally, we validate DEPET in synthetic peptide length standards, to evaluate its accuracy in measuring sub- and near-nanometer intramolecular distances. Nature Publishing Group UK 2018-11-09 /pmc/articles/PMC6226468/ /pubmed/30413716 http://dx.doi.org/10.1038/s41467-018-07218-6 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Pantazis, Antonios Westerberg, Karin Althoff, Thorsten Abramson, Jeff Olcese, Riccardo Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title | Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title_full | Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title_fullStr | Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title_full_unstemmed | Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title_short | Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
title_sort | harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6226468/ https://www.ncbi.nlm.nih.gov/pubmed/30413716 http://dx.doi.org/10.1038/s41467-018-07218-6 |
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