ArticleJournal of molecular biology2010
Protein vivisection reveals elusive intermediates in folding.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- 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
- Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Benchmarking all-atom simulations using hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Folding of a large protein at high structural resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Revealing what gets buried first in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Simplified protein models: predicting folding pathways and structure using amino acid sequences.Physical review letters · 2013Article
- Atomic-level description of ubiquitin folding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- De novo prediction of protein folding pathways and structure using the principle of sequential stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Statistical discovery of site inter-dependencies in sub-molecular hierarchical protein structuring.EURASIP journal on bioinformatics & systems biology · 2012Article
- The amino-terminal helix modulates light-activated conformational changes in AsLOV2.Journal of molecular biology · 2012Article
- X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles.Biopolymers · 2011Article
- Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH.Proteins · 2011Article
- Large shifts in pKa values of lysine residues buried inside a protein.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Ubiquitin is a novel substrate for human insulin-degrading enzyme.Journal of molecular biology · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coil.Biophysical journal · 2010Article
- Charges in the hydrophobic interior of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
2 authors.
Funding
Abstract
Although most folding intermediates escape detection, their characterization is crucial to the elucidation of folding mechanisms. Here, we outline a powerful strategy to populate partially unfolded intermediates: A buried aliphatic residue is substituted with a charged residue (e.g., Leu-->Glu(-)) to destabilize and unfold a specific region of the protein. We applied this strategy to ubiquitin, reversibly trapping a folding intermediate in which the beta5-strand is unfolded. The intermediate refolds to a native-like structure upon charge neutralization under mildly acidic conditions. Characterization of the trapped intermediate using NMR and hydrogen exchange methods identifies a second folding intermediate and reveals the order and free energies of the two major folding events on the native side of the rate-limiting step. This general strategy may be combined with other methods and have broad applications in the study of protein folding and other reactions that require trapping of high-energy states.
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