ArticleJournal of the American Chemical Society2009
Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Experimental Evidence for Millisecond-Timescale Structural Evolution Following the Microsecond-Timescale Folding of a Small Protein.Physical review letters · 2024Article
- Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A.Biochemistry · 2022Article
- Modern Kinetics and Mechanism of Protein Folding: A Retrospective.The journal of physical chemistry. B · 2021Article
- Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure.The journal of physical chemistry. B · 2021Article
- Targeting the APP-Mint2 Protein-Protein Interaction with a Peptide-Based Inhibitor Reduces Amyloid-β Formation.Journal of the American Chemical Society · 2021Article
- Theoretical analysis on thermodynamic stability of chignolin.Scientific reports · 2019Article
- Interspecies Bombolitins Exhibit Structural Diversity upon Membrane Binding, Leading to Cell Specificity.Biophysical journal · 2019Article
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Non-additive stabilization by halogenated amino acids reveals protein plasticity on a sub-angstrom scale.Protein science : a publication of the Protein Society · 2017Article
- Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017Article
- Protein unfolding mechanisms and their effects on folding experiments.F1000Research · 2017Review
- Characterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.Protein science : a publication of the Protein Society · 2016Article
- Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015Review
- Equilibrium kinetic network of the villin headpiece in implicit solvent.Biophysical journal · 2015Article
- Forces stabilizing proteins.FEBS letters · 2014Review
- Ester carbonyl vibration as a sensitive probe of protein local electric field.Angewandte Chemie (International ed. in English) · 2014Article
- Contribution of hydrogen bonds to protein stability.Protein science : a publication of the Protein Society · 2014Article
- Are current atomistic force fields accurate enough to study proteins in crowded environments?PLoS computational biology · 2014Article
- Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories.Chemical physics · 2013Article
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4 authors.
Funding
Abstract
Backbone-backbone hydrogen bonds are a common feature of native protein structures, yet their thermodynamic and kinetic influence on folding has long been debated. This is reflected by the disparity between current protein folding models, which place hydrogen bond formation at different stages along the folding trajectory. For example, previous studies have suggested that the denatured state of the villin headpiece subdomain contains a residual helical structure that may provide a bias toward the folded state by confining the conformational search associated with its folding. Although helical hydrogen bonds clearly stabilize the folded state, here we show, using an amide-to-ester mutation strategy, that the formation of backbone hydrogen bonds within helices is not rate-limiting in the folding of the subdomain, thereby suggesting that such hydrogen bonds are unlikely to be formed en route from the denatured to the transition state. On the other hand, elimination of hydrogen bonds within the turn region elicits a slower folding rate, consistent with the hypothesis that these residues are involved in the formation of a folding nucleus. While illustrating a potentially conserved aspect of helix-turn-helix folding, our results further underscore the inherent importance of turns in protein supersecondary structure formation.
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