ArticleProtein science : a publication of the Protein Society2007
Scope and utility of hydrogen exchange as a tool for mapping landscapes.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- NumSimEX: A method using EXX hydrogen exchange mass spectrometry to map the energetics of protein folding landscapes.Protein science : a publication of the Protein Society · 2025Article
- Lessons from a quarter century of being human in protein science.Protein science : a publication of the Protein Society · 2022Article
- Prediction and Validation of a Protein's Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence.Journal of chemical theory and computation · 2022Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Protein structural dynamics at the gas/water interface examined by hydrogen exchange mass spectrometry.Protein science : a publication of the Protein Society · 2015Article
- Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation.Analytical chemistry · 2013Article
- Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.The Journal of biological chemistry · 2011Article
- Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The ability to determine conformational parameters of protein-folding landscapes is critical for understanding the link between conformation, function, and disease. Monitoring hydrogen exchange (HX) of labile protons at equilibrium enables direct extraction of thermodynamic or kinetic landscape parameters in two limiting extremes. Here, we establish a quantitative framework for relating HX behavior to landscape. We use this framework to demonstrate that the range of predicted global HX behavior for the majority of a set of characterized two-state proteins under near-native conditions does not readily span between both extremes. For most, stability may be quantitatively determined under physiological conditions, with semiquantitative boundaries on kinetics additionally determined using modest experimental perturbations to shift HX behavior. The framework and relationships derived in the simple context of two-state global folding highlight the importance of understanding HX across the entire continuum of behavior, in order to apply HX to map landscapes.
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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.