Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors
Solid state nanopores are robust but the sizing can be variable, whereas protein nanopores are precisely sized but lack robustness. Here the authors cork a solid state nanopore with the DNA-translocating portal protein from the virus G20c to obtain a lipid-free hybrid nanopore that can sense various...
Guardado en:
Autores principales: | , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/216d0e35b27d41b39d8e6b39fdbece4c |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:216d0e35b27d41b39d8e6b39fdbece4c |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:216d0e35b27d41b39d8e6b39fdbece4c2021-12-02T14:39:48ZThermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors10.1038/s41467-018-07116-x2041-1723https://doaj.org/article/216d0e35b27d41b39d8e6b39fdbece4c2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07116-xhttps://doaj.org/toc/2041-1723Solid state nanopores are robust but the sizing can be variable, whereas protein nanopores are precisely sized but lack robustness. Here the authors cork a solid state nanopore with the DNA-translocating portal protein from the virus G20c to obtain a lipid-free hybrid nanopore that can sense various biopolymers.Benjamin CressiotSandra J. GreiveMehrnaz MojtabaviAlfred A. AntsonMeni WanunuNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-7 (2018) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Benjamin Cressiot Sandra J. Greive Mehrnaz Mojtabavi Alfred A. Antson Meni Wanunu Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
description |
Solid state nanopores are robust but the sizing can be variable, whereas protein nanopores are precisely sized but lack robustness. Here the authors cork a solid state nanopore with the DNA-translocating portal protein from the virus G20c to obtain a lipid-free hybrid nanopore that can sense various biopolymers. |
format |
article |
author |
Benjamin Cressiot Sandra J. Greive Mehrnaz Mojtabavi Alfred A. Antson Meni Wanunu |
author_facet |
Benjamin Cressiot Sandra J. Greive Mehrnaz Mojtabavi Alfred A. Antson Meni Wanunu |
author_sort |
Benjamin Cressiot |
title |
Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
title_short |
Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
title_full |
Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
title_fullStr |
Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
title_full_unstemmed |
Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
title_sort |
thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/216d0e35b27d41b39d8e6b39fdbece4c |
work_keys_str_mv |
AT benjamincressiot thermostablevirusportalproteinsasreprogrammableadaptersforsolidstatenanoporesensors AT sandrajgreive thermostablevirusportalproteinsasreprogrammableadaptersforsolidstatenanoporesensors AT mehrnazmojtabavi thermostablevirusportalproteinsasreprogrammableadaptersforsolidstatenanoporesensors AT alfredaantson thermostablevirusportalproteinsasreprogrammableadaptersforsolidstatenanoporesensors AT meniwanunu thermostablevirusportalproteinsasreprogrammableadaptersforsolidstatenanoporesensors |
_version_ |
1718390462326243328 |