ReviewMolecules (Basel, Switzerland)2020
Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Investigating the structural changes of myosin under high pressure processing by molecular dynamics simulations.Current research in food science · 2026Article
- Structure-guided insights into the biology of fungal effectors.The New phytologist · 2025Review
- Impact of high-pressure processing on the bioactive compounds of milk - A comprehensive review.Journal of food science and technology · 2024Review
- The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.PLoS pathogens · 2024Article
- Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance.International journal of molecular sciences · 2023Article
- The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022Review
- Biomolecules under Pressure: Phase Diagrams, Volume Changes, and High Pressure Spectroscopic Techniques.International journal of molecular sciences · 2022Review
- Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors fromInternational journal of molecular sciences · 2022Article
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 2022Article
- Proteins in Wonderland: The Magical World of Pressure.Biology · 2021Article
- Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR.Biology · 2021Article
- Special Issue-The Conformational Universe of Proteins and Peptides: Tales of Order and Disorder.Molecules (Basel, Switzerland) · 2021Article
- Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure.The journal of physical chemistry. B · 2021Article
- Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-hydrostatic pressure is an alternative perturbation method that can be used to destabilize globular proteins. Generally perfectly reversible, pressure exerts local effects on regions or domains of a protein containing internal voids, contrary to heat or chemical denaturant that destabilize protein structures uniformly. When combined with NMR spectroscopy, high pressure (HP) allows one to monitor at a residue-level resolution the structural transitions occurring upon unfolding and to determine the kinetic properties of the process. The use of HP-NMR has long been hampered by technical difficulties. Owing to the recent development of commercially available high-pressure sample cells, HP-NMR experiments can now be routinely performed. This review summarizes recent advances of HP-NMR techniques for the characterization at a quasi-atomic resolution of the protein folding energy landscape.
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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.