ArticleJournal of biomolecular NMR2011
Measurement of amide hydrogen exchange rates with the use of radiation damping.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Effects of ligand binding on dynamics of fatty acid binding protein and interactions with membranes.Biophysical journal · 2022Article
- Ligand Entry into Fatty Acid Binding Protein via Local Unfolding Instead of Gap Widening.Biophysical journal · 2020Article
- Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers.Scientific reports · 2019Article
- Atomistic Insights into the Functional Instability of the Second Helix of Fatty Acid Binding Protein.Biophysical journal · 2019Article
- Coexistence of multiple minor states of fatty acid binding protein and their functional relevance.Scientific reports · 2016Article
- Measuring hydrogen exchange in proteins by selective water saturation in (1)H- (15)N SOFAST/BEST-type experiments: advantages and limitations.Journal of biomolecular NMR · 2014Article
- Biomolecular ligands screening using radiation damping difference WaterLOGSY spectroscopy.Journal of biomolecular NMR · 2013Article
- Radiation damping in modern NMR experiments: progress and challenges.Progress in nuclear magnetic resonance spectroscopy · 2013Article
- A study on the influence of fast amide exchange on the accuracy of (15)N relaxation rate constants.Journal of biomolecular NMR · 2012Article
- Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A simple method for measuring amide hydrogen exchange rates is presented, which is based on the selective inversion of water magnetization with the use of radiation damping. Simulations show that accurate exchange rates can be measured despite the complications of radiation damping and cross relaxation to the exchange process between amide and water protons. This method cannot eliminate the contributions of the exchange-relayed NOE and direct NOE to the measured exchange rates, but minimize the direct NOE contribution. In addition, the amides with a significant amount of such indirect contributions are possible to be identified from the shape of the exchange peak intensity profiles or/and from the apparent relaxation rates of amide protons which are extracted from fitting the intensity profiles to an equation established here for our experiment. The method was tested on ubiquitin and also applied to an acyl carrier protein. The amide exchange rates for the acyl carrier protein at two pHs indicate that the entire protein is highly dynamic on the second timescale. Low protection factors for the residues in the regular secondary structural elements also suggest the presence of invisible unfolded species. The highly dynamic nature of the acyl carrier protein may be crucial for its interactions with its substrate and enzymes.
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