ArticleProtein science : a publication of the Protein Society2006
Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- SH2 Domains: Folding, Binding and Therapeutical Approaches.International journal of molecular sciences · 2022Review
- Folding and Binding Mechanisms of the SH2 Domain from Crkl.Biomolecules · 2022Article
- Characterization of early and late transition states of the folding pathway of a SH2 domain.Protein science : a publication of the Protein Society · 2022Article
- Determining folding and binding properties of the C-terminal SH2 domain of SHP2.Protein science : a publication of the Protein Society · 2021Article
- The kinetics of folding of the NSH2 domain from p85.Scientific reports · 2019Article
- Product inhibition in native-state proteolysis.PloS one · 2014Article
- Energetics-based discovery of protein-ligand interactions on a proteomic scale.Journal of molecular biology · 2011Article
- Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.Biochemistry · 2009Article
- Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange.Journal of molecular biology · 2008Article
- Conformational equilibria and rates of localized motion within hepatitis B virus capsids.Journal of molecular biology · 2008Article
- Folding versus aggregation: polypeptide conformations on competing pathways.Archives of biochemistry and biophysics · 2008Review
- Anatomy of energetic changes accompanying urea-induced protein denaturation.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The folding energy landscape of the dimerization domain of Escherichia coli Trp repressor: a joint experimental and theoretical investigation.Journal of molecular biology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have defined the free-energy profile of the Src SH2 domain using a variety of biophysical techniques. Equilibrium and kinetic experiments monitored by tryptophan fluorescence show that Src SH2 is quite stable and folds rapidly by a two-state mechanism, without populating any intermediates. Native state hydrogen-deuterium exchange confirms this two-state behavior; we detect no cooperative partially unfolded forms in equilibrium with the native conformation under any conditions. Interestingly, the apparent stability of the protein from hydrogen exchange is 2 kcal/mol greater than the stability determined by both equilibrium and kinetic studies followed by fluorescence. Native-state proteolysis demonstrates that this "super protection" does not result from a deviation from the linear extrapolation model used to fit the fluorescence data. Instead, it likely arises from a notable compaction in the unfolded state under native conditions, resulting in an ensemble of conformations with substantial solvent exposure of side chains and flexible regions sensitive to proteolysis, but backbone amides that exchange with solvent approximately 30-fold slower than would be expected for a random coil. The apparently simple behavior of Src SH2 in traditional unfolding studies masks the significant complexity present in the denatured-state ensemble.
Indexed as
Identifiers
What OpenQuestion holds
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.