Engineering a nanopore with co-chaperonin function-Reference-Cited by-同舟云学术

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Engineering a nanopore with co-chaperonin function

Published:2015-12-04 Issue:11 Volume:1 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Ho Ching-Wen¹,Van Meervelt Veerle¹,Tsai Keng-Chang²,De Temmerman Pieter-Jan³^ORCID,Mast Jan³^ORCID,Maglia Giovanni⁴

Affiliation:

1. Department of Chemistry, University of Leuven, Leuven 3001, Belgium.

2. National Research Institute of Chinese Medicine, Ministry of Health and Welfare, Taipei 11221, Taiwan.

3. Electron Microscopy Unit, Veterinary and Agrochemical Research Centre (CODA-CERVA), Brussels 1180, Belgium.

4. Groningen Biotechnology Institute, University of Groningen, Groningen 9747AG, Netherlands.

Abstract

A recombinant GroES nanopore reveals the dynamics and kinetics of the allosteric intermediates of the GroEL protein-folding reaction.

Funder

European Research Council

Fonds Wetenschappelijk Onderzoek

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference63 articles.

1. DNA strands from denatured duplexes are translocated through engineered protein nanopores at alkaline pH;Maglia G.;Nano Lett.,2009

2. Urea facilitates the translocation of single-stranded DNA and RNA through the α-hemolysin nanopore;Japrung D.;Biophys. J.,2010

3. A protein rotaxane controls the translocation of proteins across a ClyA nanopore;Biesemans A.;Nano Lett.,2015

4. Single DNA rotaxanes of a transmembrane pore protein;Sánchez-Quesada J.;Angew. Chem. Int. Ed.,2004

5. Counting polymers moving through a single ion channel;Bezrukov S. M.;Nature,1994

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