ArticleProceedings of the National Academy of Sciences of the United States of America2009
Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. 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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10 citing papers in PubMed.
- Protein Structural Characterization Using Electron Transfer Dissociation and Hydrogen Exchange-Mass Spectrometry.Bio-protocol · 2025Article
- Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein.Protein science : a publication of the Protein Society · 2022Article
- Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein.eLife · 2019Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.Biophysical journal · 2013Article
- Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.Journal of the American Chemical Society · 2013Article
- Characterization of deamidation of barstar using electrospray ionization quadrupole time-of-flight mass spectrometry, which stabilizes an equilibrium unfolding intermediate.Protein science : a publication of the Protein Society · 2012Article
- Structural and kinetic mapping of side-chain exposure onto the protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Plasticity of cytochrome P450 2B4 as investigated by hydrogen-deuterium exchange mass spectrometry and X-ray crystallography.The Journal of biological chemistry · 2010Article
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2 authors.
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Abstract
Little is known about the role of protein dynamics in directing protein unfolding along a specific pathway and about the role played by chemical denaturants in modulating the dynamics and the initiation of unfolding. In this study, deuterium-hydrogen exchange (HX) detected by electrospray ionization mass spectrometry (ESI-MS) was used to study the unfolding of the SH3 domain of the PI3 kinase. Unfolding on the principal unfolding pathway occurs in 2 steps, both in the absence and in the presence of 1.8 M guanidine hydrochloride (GdnHCl). In both cases, the first step leads to the formation of an intermediate, I(N), with 5 fewer protected amide hydrogen sites than in N. In the second step, I(N) loses the structure protecting the remaining 14 amide hydrogen sites from HX as it unfolds completely. ESI-MS analysis of fragments of the protein created by proteolytic digestion, after completion of the HX reaction, shows that I(N) has lost protection against HX in the same segments of native structure during unfolding in the absence and presence of 1.8 M GdnHCl. Hence, GdnHCl does not appear to play a direct active role in the initiation of unfolding. However, at higher GdnHCl concentrations, a second unfolding pathway is shown to compete effectively with the N <--> I(N) <--> U pathway. In this way, the denaturant modulates the energy landscape of unfolding.
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