ArticleProceedings of the National Academy of Sciences of the United States of America2015
Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
- Quantifying the Characteristic Turnover Frequency of an Individual Redox Enzyme via Real-Time Electrical Transduction of Catalytic Events in a Label-Free Single-Protein Junction.Journal of the American Chemical Society · 2026Article
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Up- and Down-Regulation of Enzyme Activity in Aggregates with Gold-Covered Magnetic Nanoparticles Triggered by Low-Frequency Magnetic Field.Nanomaterials (Basel, Switzerland) · 2024Article
- Statistical Improvement of rGILCC 1 and rPOXA 1B Laccases Activity Assay Conditions Supported by Molecular Dynamics.Molecules (Basel, Switzerland) · 2023Article
- Progression of Antiviral Agents Targeting Viral Polymerases.Molecules (Basel, Switzerland) · 2022Review
- Article
- Multiplexed single-molecule force spectroscopy for dissecting biophysical regulation of membrane receptors functions on live cells.Biophysics reports · 2021Article
- Shifting Retroviral Vector Integrations Away from Transcriptional Start Sites via DNA-Binding Protein Domain Insertion into Integrase.Molecular therapy. Methods & clinical development · 2019Article
- Soleus muscle H-reflex monitoring in endoscopic surgery under general anesthesia percutaneous interlaminar approach.Experimental and therapeutic medicine · 2018Article
- Article
- Probing conformational dynamics of an enzymatic active site by an in situ single fluorogenic probe under piconewton force manipulation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterizing the impact of fluctuating enzyme conformation on enzymatic activity is critical in understanding the structure-function relationship and enzymatic reaction dynamics. Different from studying enzyme conformations under a denaturing condition, it is highly informative to manipulate the conformation of an enzyme under an enzymatic reaction condition while monitoring the real-time enzymatic activity changes simultaneously. By perturbing conformation of horseradish peroxidase (HRP) molecules using our home-developed single-molecule total internal reflection magnetic tweezers, we successfully manipulated the enzymatic conformation and probed the enzymatic activity changes of HRP in a catalyzed H2O2-amplex red reaction. We also observed a significant tolerance of the enzyme activity to the enzyme conformational perturbation. Our results provide a further understanding of the relation between enzyme behavior and enzymatic conformational fluctuation, enzyme-substrate interactions, enzyme-substrate active complex formation, and protein folding-binding interactions.
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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.