ArticleJournal of the American Chemical Society2010
Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Kinetic Dissection of Proton-Coupled Conformational Transitions in Nucleic Acids by Integrating pH-Dependent NMR and Chemical Modifications.Journal of the American Chemical Society · 2025Article
- Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins.Biophysics and physicobiology · 2023Article
- Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β.Frontiers in molecular biosciences · 2021Article
- 2'-O-Methylation can increase the abundance and lifetime of alternative RNA conformational states.Nucleic acids research · 2020Article
- Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch.Nature communications · 2016Article
- A dynamic look backward and forward.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Review
- Article
- Fast protein folding kinetics.Quarterly reviews of biophysics · 2014Review
- Chemical exchange in biomacromolecules: past, present, and future.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Fast photochemical oxidation of proteins and mass spectrometry follow submillisecond protein folding at the amino-acid level.Journal of the American Chemical Society · 2012Article
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains.Journal of biomolecular NMR · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Proteins that fold rapidly, on the (sub-) microsecond time scale, offer the prospect of direct comparison between experimental data and molecular dynamics simulations. However, experimental studies for such proteins frequently are hindered because folding rates are too fast to measure using conventional stopped-flow methods. To overcome this impediment, NMR spin relaxation dispersion experiments are used to quantify mutational effects on kinetics (DeltaDeltaG(o)), stability (DeltaDeltaG(o)), and phi-values (DeltaDeltaG(dagger)/DeltaDeltaG(o)) for proteins exhibiting chemical exchange line broadening that is fast on the NMR chemical shift time scale. The accuracy of phi-value analysis is enhanced because mutational effects on denatured or intermediate states can be detected through changes in line broadening. The transition and intermediate states of the villin headpiece domain, HP67, are characterized in varying solvent conditions to validate the method.
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