Evidence map›Paper›PMID 28435868›Full record

ArticleScience advances2017

Label-free optical detection of single enzyme-reactant reactions and associated conformational changes.

Eugene Kim, Martin D Baaske, Isabel Schuldes, Peter S Wilsch, Frank Vollmer

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Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed.

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  16. Photothermal Spectro-Microscopy as Benchmark for Optoplasmonic Bio-Detection Assays.The journal of physical chemistry. C, Nanomaterials and interfaces · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Eugene KimMax Planck Institute for the Science of Light, Staudtstrasse 2, 91058 Erlangen, Germany.
Martin D BaaskeMax Planck Institute for the Science of Light, Staudtstrasse 2, 91058 Erlangen, Germany.
Isabel SchuldesMax Planck Institute for the Science of Light, Staudtstrasse 2, 91058 Erlangen, Germany.
Peter S WilschMax Planck Institute for the Science of Light, Staudtstrasse 2, 91058 Erlangen, Germany.ORCID 0000-0002-4395-8919
Frank VollmerMax Planck Institute for the Science of Light, Staudtstrasse 2, 91058 Erlangen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monitoring the kinetics and conformational dynamics of single enzymes is crucial to better understand their biological functions because these motions and structural dynamics are usually unsynchronized among the molecules. However, detecting the enzyme-reactant interactions and associated conformational changes of the enzyme on a single-molecule basis remains as a challenge to established optical techniques because of the commonly required labeling of the reactants or the enzyme itself. The labeling process is usually nontrivial, and the labels themselves might skew the physical properties of the enzyme. We demonstrate an optical, label-free method capable of observing enzymatic interactions and associated conformational changes on a single-molecule level. We monitor polymerase/DNA interactions via the strong near-field enhancement provided by plasmonic nanorods resonantly coupled to whispering gallery modes in microcavities. Specifically, we use two different recognition schemes: one in which the kinetics of polymerase/DNA interactions are probed in the vicinity of DNA-functionalized nanorods, and the other in which these interactions are probed via the magnitude of conformational changes in the polymerase molecules immobilized on nanorods. In both approaches, we find that low and high polymerase activities can be clearly discerned through their characteristic signal amplitude and signal length distributions. Furthermore, the thermodynamic study of the monitored interactions suggests the occurrence of DNA polymerization. This work constitutes a proof-of-concept study of enzymatic activities using plasmonically enhanced microcavities and establishes an alternative and label-free method capable of investigating structural changes in single molecules.

Indexed as

Models, ChemicalDNADNA-Directed DNA PolymeraseNanotubesProtein ConformationDNADNA-Directed DNA Polymeraseconformational changeoptical microcavitypolymeraseprotein-DNA interactionssingle enzyme dynamicssingle molecule reactionwhispering Gallery mode

Identifiers

PMID28435868
PMCPMC5371424

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.