ArticleProceedings of the National Academy of Sciences of the United States of America2010
Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A.Biochemistry · 2022Article
- Article
- Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Biochemistry · 2021Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Controlling Structure and Dimensions of a Disordered Protein via Mutations.Biochemistry · 2020Article
- Local and non-local topological information in the denatured state ensemble of a β-barrel protein.Protein science : a publication of the Protein Society · 2018Article
- Entropic Control of an Excited Folded-Like Conformation in a Disordered Protein Ensemble.Journal of molecular biology · 2018Article
- Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Journal of molecular biology · 2018Article
- 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
- EPI-001, A Compound Active against Castration-Resistant Prostate Cancer, Targets Transactivation Unit 5 of the Androgen Receptor.ACS chemical biology · 2016Article
- Article
- Nascent β-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts.Biophysical journal · 2015Article
- A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Protein science : a publication of the Protein Society · 2014Article
- Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1.Scientific reports · 2014Article
- Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment.Journal of the American Chemical Society · 2012Article
- Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop end.Biochemistry · 2012Article
- Conformational properties of the unfolded state of Im7 in nondenaturing conditions.Journal of molecular biology · 2012Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts.Protein science : a publication of the Protein Society · 2011Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In studies of the ensembles of unfolded structures of a four-helix bundle protein, we have detected the presence of potential precursors of native tertiary structures. These observations were based on the perturbation of NMR chemical shifts of the protein backbone atoms by single site mutations. Some mutations change the chemical shifts of residues remote from the site of mutation indicating the presence of an interaction between the mutated and the remote residues, suggesting that the formation of helix segments and helix-helix interactions is cooperative. We can begin to track down the folding mechanism of this protein using only experimental data by combining the information available for the rate limiting structure formation during the folding process with measurements of the site specific hydrogen bond formation in the burst phase, and with the existence prior to the folding reaction of tertiary structures in the ensemble of otherwise unfolded structures observed in the present study.
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