Dynamics of single enzymes confined inside a nanopore
Galenkamp, Nicole Stéphanie LU
; van den Noort, Marco
and Maglia, Giovanni
(2025)
In RSC Chemical Biology
- Abstract
Enzymes are powerful catalysts that perform chemical reactions with remarkable speed and specificity. Their intrinsic dynamics often play a crucial role in determining their catalytic properties. To achieve a comprehensive understanding of enzymes, a diverse and sophisticated experimental toolbox capable of studying enzyme dynamics at the single-molecule level is necessary. In this review, we discuss nanopore technology as an emerging and powerful platform in single-molecule enzymology. We demonstrate how nanopores can be employed to probe enzyme dynamics in real-time, and we highlight how these studies have contributed to fundamentally and quantitatively elucidating enzymological concepts, such as allostery and hysteresis. Finally, we... (More)
Enzymes are powerful catalysts that perform chemical reactions with remarkable speed and specificity. Their intrinsic dynamics often play a crucial role in determining their catalytic properties. To achieve a comprehensive understanding of enzymes, a diverse and sophisticated experimental toolbox capable of studying enzyme dynamics at the single-molecule level is necessary. In this review, we discuss nanopore technology as an emerging and powerful platform in single-molecule enzymology. We demonstrate how nanopores can be employed to probe enzyme dynamics in real-time, and we highlight how these studies have contributed to fundamentally and quantitatively elucidating enzymological concepts, such as allostery and hysteresis. Finally, we explore the potentials and limitations of nanopores in advancing single-molecule enzymology. By presenting the unique possibilities offered by nanopores, we aim to inspire the integration of this technology into future enzymology research.
(Less)
- author
- Galenkamp, Nicole Stéphanie
LU
; van den Noort, Marco
and Maglia, Giovanni
- organization
- publishing date
- 2025
- type
- Contribution to journal
- publication status
- epub
- subject
- in
- RSC Chemical Biology
- publisher
- Royal Society of Chemistry
- external identifiers
-
- scopus:105018644793
- pmid:40978460
- ISSN
- 2633-0679
- DOI
- 10.1039/d5cb00149h
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2025 RSC.
- id
- 763e470d-0e71-499f-8f0b-098bda813502
- date added to LUP
- 2026-01-26 09:55:03
- date last changed
- 2026-01-27 03:00:08
@article{763e470d-0e71-499f-8f0b-098bda813502,
abstract = {{<p>Enzymes are powerful catalysts that perform chemical reactions with remarkable speed and specificity. Their intrinsic dynamics often play a crucial role in determining their catalytic properties. To achieve a comprehensive understanding of enzymes, a diverse and sophisticated experimental toolbox capable of studying enzyme dynamics at the single-molecule level is necessary. In this review, we discuss nanopore technology as an emerging and powerful platform in single-molecule enzymology. We demonstrate how nanopores can be employed to probe enzyme dynamics in real-time, and we highlight how these studies have contributed to fundamentally and quantitatively elucidating enzymological concepts, such as allostery and hysteresis. Finally, we explore the potentials and limitations of nanopores in advancing single-molecule enzymology. By presenting the unique possibilities offered by nanopores, we aim to inspire the integration of this technology into future enzymology research.</p>}},
author = {{Galenkamp, Nicole Stéphanie and van den Noort, Marco and Maglia, Giovanni}},
issn = {{2633-0679}},
language = {{eng}},
publisher = {{Royal Society of Chemistry}},
series = {{RSC Chemical Biology}},
title = {{Dynamics of single enzymes confined inside a nanopore}},
url = {{http://dx.doi.org/10.1039/d5cb00149h}},
doi = {{10.1039/d5cb00149h}},
year = {{2025}},
}