ArticleThe journal of physical chemistry. B2011
Direct assessment of the α-helix nucleation time.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Enhanced statistical sampling reveals microscopic complexity in the talin mechanosensor folding energy landscape.Nature physics · 2023Article
- Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study.The journal of physical chemistry. B · 2019Article
- Simultaneous Determination of Two Subdomain Folding Rates Using the "Transfer-Quench" Method.Biophysical journal · 2017Article
- Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017Article
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
- Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics.Biophysical journal · 2016Article
- Tuning the Attempt Frequency of Protein Folding Dynamics via Transition-State Rigidification: Application to Trp-Cage.The journal of physical chemistry letters · 2015Article
- Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.Science China. Chemistry · 2014Article
- Molecular basis of the mechanical hierarchy in myomesin dimers for sarcomere integrity.Biophysical journal · 2014Article
- 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
- Solvent-Exposed Salt Bridges Influence the Kinetics of α-Helix Folding and Unfolding.The journal of physical chemistry letters · 2014Article
- Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Journal of the American Chemical Society · 2013Article
- Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B.Biochemistry · 2012Article
- Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation.Biophysical journal · 2012Article
- Di-Cysteine S,S-Tetrazine: A Potential Ultra-fast Photochemical Trigger to Explore the Early Events of Peptide/Protein Folding.Journal of photochemistry and photobiology. A, Chemistry · 2012Article
- Residue-specific α-helix propensities from molecular simulation.Biophysical journal · 2012Article
- Achieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.Angewandte Chemie (International ed. in English) · 2011Article
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3 authors.
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Abstract
The nucleation event in α-helix formation is a fundamental process in protein folding. However, determining how quickly it takes place based on measurements of the relaxation dynamics of helical peptides is difficult because such relaxations invariably contain contributions from various structural transitions such as from helical to nonhelical states and helical to partial-helical conformations. Herein, we measure the temperature-jump (T-jump) relaxation kinetics of three model peptides that fold into a single-turn α-helix, using time-resolved infrared spectroscopy, aiming to provide a direct assessment of the helix nucleation rate. The α-helical structure of these peptides is stabilized by a covalent cross-linker formed between the side chains of two residues at the i and i + 4 positions. If we assume that this cross-linker mimics the structural constraint arising from a strong side chain-side chain interaction (e.g., a salt bridge) in proteins, these peptides would represent good models for studying the nucleation process of an α-helix in a protein environment. Indeed, we find that the T-jump induced relaxation rate of these peptides is approximately (0.6 μs)(-1) at room temperature, which is slower than that of commonly studied alanine-based helical peptides but faster than that of a naturally occurring α-helix whose folded state is stabilized by a series of side chain-side chain interactions. Taken together, our results put an upper limit of about 1 μs for the helix nucleation time at 20 °C and suggest that the subsequent propagation steps occur with a time constant of about 240 ns.
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