The Manipulation of the Internal Hydrophobicity of FraC Nanopores Augments Peptide Capture and Recognition-Reference-Cited by-同舟云学术

The Manipulation of the Internal Hydrophobicity of FraC Nanopores Augments Peptide Capture and Recognition

Published:2021-06-01 Issue:6 Volume:15 Page:9600-9613
ISSN:1936-0851
Container-title:ACS Nano
language:en
Short-container-title:ACS Nano

Author:

Lucas Florian Leonardus Rudolfus¹^ORCID,Sarthak Kumar²,Lenting Erica Mariska¹,Coltan David¹,van der Heide Nieck Jordy¹,Versloot Roderick Corstiaan Abraham¹,Aksimentiev Aleksei³^ORCID,Maglia Giovanni¹^ORCID

Affiliation:

1. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands

2. Center for Biophysics and Quantitative Biology, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, United States

3. Department of Physics, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, United States

Funder

Stichting voor Fundamenteel Onderzoek der Materie

National Institute of General Medical Sciences

H2020 European Research Council

Division of Physics

Publisher

American Chemical Society (ACS)

Subject

General Physics and Astronomy,General Engineering,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/acsnano.0c09958

Reference65 articles.

1. Electrical recognition of the twenty proteinogenic amino acids using an aerolysin nanopore

2. Discrimination of oligonucleotides of different lengths with a wild-type aerolysin nanopore

3. Single-Molecule Analyte Recognition with ClyA Nanopores Equipped with Internal Protein Adaptors

4. Characterization of individual polynucleotide molecules using a membrane channel

5. Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter

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