ArticleBiochemistry2009
The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A.Biochemistry · 2022Article
- Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates.Biophysical journal · 2019Article
- Modeling of Disordered Protein Structures Using Monte Carlo Simulations and Knowledge-Based Statistical Force Fields.International journal of molecular sciences · 2019Review
- Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.Biophysical journal · 2018Article
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation.Journal of the American Chemical Society · 2015Article
- Advances in turbulent mixing techniques to study microsecond protein folding reactions.Biopolymers · 2013Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering.Biopolymers · 2011Review
- Counting peptide-water hydrogen bonds in unfolded proteins.Protein science : a publication of the Protein Society · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- Taming the complexity of protein folding.Current opinion in structural biology · 2011Review
- Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding.Biophysical journal · 2010Article
- Protein folded states are kinetic hubs.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins.Protein science : a publication of the Protein Society · 2010Article
- The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure.Journal of the American Chemical Society · 2010Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
Interest in the structural and dynamic properties of unfolded proteins has increased in recent years owing to continued interest in protein folding and misfolding. Knowledge of the unfolded state under native conditions is particularly important for obtaining a complete picture of the protein folding process. The C-terminal domain of protein L9 is a globular alpha, beta protein with an unusual mixed parallel and antiparallel beta-strand structure. The folding kinetics and equilibrium unfolding of CTL9 strongly depend on pH, and follow a simple two state model. Both the native and the unfolded state can be significantly populated at pH 3.8 in the absence of denaturant, allowing the native state and the unfolded state to be characterized under identical conditions. Backbone (15)N, (13)C, (1)H and side-chain (13)C(beta), (1)H(beta) chemical shifts, amide proton NOEs, and (15)N R(2) relaxation rates were obtained for the two conformational states at pH 3.8. All the data indicate that the pH 3.8 native state is well folded and is similar to the native state at neutral pH. There is significant residual structure in the pH 3.8 unfolded state. The regions corresponding to the two native state alpha-helices show strong preference to populate helical phi and psi angles. The segment that connects alpha-helix 2 and beta-strand 2 has a significant tendency to form non-native alpha-helical structure. Comparison with the pH 2.0 unfolded state and the urea unfolded state indicates that the tendency to adopt both native and non-native helical structure is stronger at pH 3.8, demonstrating that the unfolded state of CTL9 under native-like conditions is more structured. The implications for the folding of CTL9 are discussed.
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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.