ArticleProceedings of the National Academy of Sciences of the United States of America2013
Testing the diffusing boundary model for the helix-coil transition in peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Article
- The Iconic α-Helix: From Pauling to the Present.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- Length Dependent Folding Kinetics of Alanine-Based Helical Peptides from Optimal Dimensionality Reduction.Life (Basel, Switzerland) · 2021Article
- Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Spreading of perturbations in myosin group kinetics along actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering.The journal of physical chemistry. B · 2019Article
- Article
- Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017Article
- A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.Biophysical journal · 2015Article
- Effects of side chains in helix nucleation differ from helix propagation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Transition state and ground state properties of the helix-coil transition in peptides deduced from high-pressure studies.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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5 authors.
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Abstract
The dynamics of peptide α-helices have been studied extensively for many years, and the kinetic mechanism of the helix-coil dynamics has been discussed controversially. Recent experimental results have suggested that equilibrium helix-coil dynamics are governed by movement of the helix/coil boundary along the peptide chain, which leads to slower unfolding kinetics in the helix center compared with the helix ends and position-independent helix formation kinetics. We tested this diffusion of boundary model in helical peptides of different lengths by triplet-triplet energy transfer measurements and compared the data with simulations based on a kinetic linear Ising model. The results show that boundary diffusion in helical peptides can be described by a classical, Einstein-type, 1D diffusion process with a diffusion coefficient of 2.7⋅10(7) (amino acids)(2)/s or 6.1⋅10(-9) cm(2)/s. In helices with a length longer than about 40 aa, helix unfolding by coil nucleation in a helical region occurs frequently in addition to boundary diffusion. Boundary diffusion is slowed down by helix-stabilizing capping motifs at the helix ends in agreement with predictions from the kinetic linear Ising model. We further tested local and nonlocal effects of amino acid replacements on helix-coil dynamics. Single amino acid replacements locally affect folding and unfolding dynamics with a ϕf-value of 0.35, which shows that interactions leading to different helix propensities for different amino acids are already partially present in the transition state for helix formation. Nonlocal effects of amino acid replacements only influence helix unfolding (ϕf = 0) in agreement with a diffusing boundary mechanism.
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