Nicole Stéphanie Galenkamp
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View article: Author Correction: Allostery can convert binding free energies into concerted domain motions in enzymes
Author Correction: Allostery can convert binding free energies into concerted domain motions in enzymes Open
Correction to: Nature Communicationshttps://doi.org/10.1038/s41467-024-54421-9, published online 22 November 2024 In this article the author’s name Andreas Milias-Argeitis was incorrectly written as Andreas Milias Argeitis. The original ar…
View article: Dynamics of single enzymes confined inside a nanopore
Dynamics of single enzymes confined inside a nanopore Open
This review discusses nanopore technology as an emerging and powerful platform in single-molecule enzymology, highlighting its previous contributions to the field and exploring its future potential.
View article: Allostery can convert binding free energies into concerted domain motions in enzymes
Allostery can convert binding free energies into concerted domain motions in enzymes Open
Enzymes’ mechanisms are typically inferred from structural data. However, understanding proteins’ functions requires unravelling the intricate dynamic interplay between dynamics, conformational substates and multiple protein structures. He…
View article: Specific Detection of Proteins by a Nanobody-Functionalized Nanopore Sensor
Specific Detection of Proteins by a Nanobody-Functionalized Nanopore Sensor Open
Nanopores are label-free single-molecule analytical tools that show great potential for stochastic sensing of proteins. Here, we described a ClyA nanopore functionalized with different nanobodies through a 5-6 nm DNA linker at its peripher…
View article: Hypothesis-Driven, Structure-Based Design in Photopharmacology: The Case of eDHFR Inhibitors
Hypothesis-Driven, Structure-Based Design in Photopharmacology: The Case of eDHFR Inhibitors Open
Photopharmacology uses light to regulate the biological activity of drugs. This precise control is obtained through the incorporation of molecular photoswitches into bioactive molecules. A major challenge for photopharmacology is the ratio…
View article: Single-Molecule Sampling of Dihydrofolate Reductase Shows Kinetic Pauses and an Endosteric Effect Linked to Catalysis
Single-Molecule Sampling of Dihydrofolate Reductase Shows Kinetic Pauses and an Endosteric Effect Linked to Catalysis Open
The ability to sample multiple reactions on the same single enzyme is important to link rare intermediates with catalysis and to unravel the role of conformational changes. Despite decades of efforts, however, the single-molecule character…
View article: Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore Sensor
Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore Sensor Open
The ability to measure the concentration of metabolites in biological samples is important, both in the clinic and for home diagnostics. Here we present a nanopore‐based biosensor and automated data analysis for quantification of thiamine …
View article: Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore Sensor
Automated Electrical Quantification of Vitamin B1 in a Bodily Fluid using an Engineered Nanopore Sensor Open
The ability to measure the concentration of metabolites in biological samples is important, both in the clinic and for home diagnostics. Here we present a nanopore‐based biosensor and automated data analysis for quantification of thiamine …
View article: Mechanism of Resistance Development in E. coli against TCAT, a Trimethoprim-Based Photoswitchable Antibiotic
Mechanism of Resistance Development in E. coli against TCAT, a Trimethoprim-Based Photoswitchable Antibiotic Open
During the last decades, a continuous rise of multi-drug resistant pathogens has threatened antibiotic efficacy. To tackle this key challenge, novel antimicrobial therapies are needed with increased specificity for the site of infection. P…
View article: Single-molecule enzymology with a ClyA nanopore
Single-molecule enzymology with a ClyA nanopore Open
The goal of this thesis was to use nanopore measurements to study enzymes at the single-molecule level. We started by developing a nanopore sensor based on a protein lodged inside the ClyA nanopore, so that the concentration of glucose and…
View article: Substrate binding and turnover modulate the affinity landscape of dihydrofolate reductase to increase its catalytic efficiency
Substrate binding and turnover modulate the affinity landscape of dihydrofolate reductase to increase its catalytic efficiency Open
It is generally accepted that enzymes structures evolved to stabilize the transition-state of a catalyzed reaction. Here, observing single molecules with a multi-turnover resolution, we provide experimental evidence for a more sophisticate…
View article: Current Blockades of Proteins inside Nanopores for Real-Time Metabolome Analysis
Current Blockades of Proteins inside Nanopores for Real-Time Metabolome Analysis Open
Biological nanopores are emerging as powerful and low-cost sensors for real-time analysis of biological samples. Proteins can be incorporated inside the nanopore, and ligand binding to the protein adaptor yields changes in nanopore conduct…
View article: Single-molecule enzymology with a ClyA nanopore
Single-molecule enzymology with a ClyA nanopore Open
The goal of this thesis was to use nanopore measurements to study enzymes at the single-molecule level. We started by developing a nanopore sensor based on a protein lodged inside the ClyA nanopore, so that the concentration of glucose and…
View article: Engineering and Modeling the Electrophoretic Trapping of a Single Protein Inside a Nanopore
Engineering and Modeling the Electrophoretic Trapping of a Single Protein Inside a Nanopore Open
The ability to confine and to study single molecules has enabled important advances in natural and applied sciences. Recently, we have shown that unlabeled proteins can be confined inside the biological nanopore Cytolysin A (ClyA) and conf…