ArticleNature communications2020
Studying biomolecular folding and binding using temperature-jump mass spectrometry.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 50 citations in OpenAlex.
- Native-Like Protein Structures in Vacuo: Steric Cooperativity as a Kinetic Barrier to Denaturation.JACS Au · 2026Article
- Determination of Thermochemical Barriers in Multiple-Collision-Induced Dissociation Experiments on Gas-Phase Protein Complexes.Journal of the American Chemical Society · 2025Article
- Traversing the drug discovery landscape using native mass spectrometry.Current opinion in structural biology · 2025Review
- Gas-Phase Fragmentation as a Probe of G-Quadruplex Formation.Analytical chemistry · 2023Article
- Determining the gas-phase structures of α-helical peptides from shape, microsolvation, and intramolecular distance data.Nature communications · 2023Article
- Article
- Collagen-Sealed Polyester Vascular Prostheses Functionalized by Polycatecholamine Coatings.International journal of molecular sciences · 2022Article
- Refolding of Lysozyme in Glycerol as Studied by Fast Scanning Calorimetry.International journal of molecular sciences · 2022Article
- Temperature Regulates Stability, Ligand Binding (MgJournal of the American Chemical Society · 2022Article
- High-Throughput Native Mass Spectrometry Screening in Drug Discovery.Frontiers in molecular biosciences · 2022Review
- Temperature-Controlled Electrospray Ionization: Recent Progress and Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Combining Electrospray Mass Spectrometry (ESI-MS) and Computational Techniques in the Assessment of G-Quadruplex Ligands: A Hybrid Approach to Optimize Hit Discovery.Journal of medicinal chemistry · 2021Article
- Thermal Analysis of a Mixture of Ribosomal Proteins by vT-ESI-MS: Toward a Parallel Approach for Characterizing theAnalytical chemistry · 2021Article
- Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding.Analytical chemistry · 2021Article
- Plasmonic Layer as a Localized Temperature Control Element for Surface Plasmonic Resonance-Based Sensors.Sensors (Basel, Switzerland) · 2021Article
- Temperature-Jump 2D IR Spectroscopy with Intensity-Modulated CW Optical Heating.The journal of physical chemistry. B · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Characterizing folding and complex formation of biomolecules provides a view into their thermodynamics, kinetics and folding pathways. Deciphering kinetic intermediates is particularly important because they can often be targeted by drugs. The key advantage of native mass spectrometry over conventional methods that monitor a single observable is its ability to identify and quantify coexisting species. Here, we show the design of a temperature-jump electrospray source for mass spectrometry that allows one to perform fast kinetics experiments (0.16-32 s) at different temperatures (10-90 °C). The setup allows recording of both folding and unfolding kinetics by using temperature jumps from high to low, and low to high, temperatures. Six biological systems, ranging from peptides to proteins to DNA complexes, exemplify the use of this device. Using temperature-dependent experiments, the folding and unfolding of a DNA triplex are studied, providing detailed information on its thermodynamics and kinetics.
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Registered trials
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.