ArticleProtein science : a publication of the Protein Society2012
Protein dynamics viewed by hydrogen exchange.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed.
- Article
- Use of hydrogen deuterium exchange mass spectrometry in tandem with modern structural biology.The Biochemical journal · 2026Review
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.Journal of the American Chemical Society · 2026Article
- High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026Article
- How the non-motile kinesin KIF7 adapts conserved kinesin principles for its function in Hedgehog signaling.bioRxiv : the preprint server for biology · 2026Article
- Site-resolved energetic information from HX-MS experiments.Nature chemical biology · 2026Article
- Hydrogen Exchange Mass Spectrometry (HX-MS) for Mapping Antibody Binding Sites and Conformational Dynamics of ADAMTS13.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Ensemble Basis of Allostery and Function: Insights from Models of Local Unfolding.Journal of molecular biology · 2025Review
- Identification of a direct interaction between the Fab domains of IgG antibodies and human FcRn upon IgG-FcRn complex formation.Communications biology · 2025Article
- Mapping the structural heterogeneity of Pup ligase PafA using H/D exchange mass spectrometry.The Journal of biological chemistry · 2025Article
- Mechanism of allosteric activation in human mitochondrial ClpP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the CNOT1(800-999) HEAT Domain and Its Interactions with Tristetraprolin (TTP) as Revealed by Hydrogen/Deuterium Exchange Mass Spectrometry.Biomolecules · 2025Article
- Serine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein Microarrays for High Throughput Hydrogen/Deuterium Exchange Monitored by FTIR Imaging.International journal of molecular sciences · 2024Article
- Investigation of the Solid-State Interactions in Lyophilized Human G-CSF Using Hydrogen-Deuterium Exchange Mass Spectrometry.Molecular pharmaceutics · 2024Article
- Article
- Hydrogen Deuterium Exchange and other Mass Spectrometry-based Approaches for Epitope Mapping.Frontiers in analytical science · 2023Article
- ATR-FTIR Biosensors for Antibody Detection and Analysis.International journal of molecular sciences · 2022Article
- Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly.Nucleic acids research · 2022Article
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature.Science advances · 2022Article
38 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
To examine the relationship between protein structural dynamics and measurable hydrogen exchange (HX) data, the detailed exchange behavior of most of the backbone amide hydrogens of Staphylococcal nuclease was compared with that of their neighbors, with their structural environment, and with other information. Results show that H-bonded hydrogens are protected from exchange, with HX rate effectively zero, even when they are directly adjacent to solvent. The transition to exchange competence requires a dynamic structural excursion that removes H-bond protection and allows exposure to solvent HX catalyst. The detailed data often make clear the nature of the dynamic excursion required. These range from whole molecule unfolding, through smaller cooperative unfolding reactions of secondary structural elements, and down to local fluctuations that involve as little as a single peptide group or side chain or water molecule. The particular motion that dominates the exchange of any hydrogen is the one that allows the fastest HX rate. The motion and the rate it produces are determined by surrounding structure and not by nearness to solvent or the strength of the protecting H-bond itself or its acceptor type (main chain, side chain, structurally bound water). Many of these motions occur over time scales that are appropriate for biochemical function.
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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.