ArticleProceedings of the National Academy of Sciences of the United States of America2004
Understanding the key factors that control the rate of beta-hairpin folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Signatures of protein fold switching in the unfolded state.Biophysical journal · 2026Article
- 3β-Corner Stability by Comparative Molecular Dynamics Simulations.International journal of molecular sciences · 2022Article
- Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry.Chemical reviews · 2022Review
- The B1 Domain of Streptococcal Protein G Serves as a Multi-Functional Tag for Recombinant Protein Production in Plants.Frontiers in plant science · 2022Article
- Template-assisted design of monomeric polyQ models to unravel the unique role of glutamine side chains in disease-related aggregation.Chemical science · 2021Article
- Enhanced Sensitivity to Local Dynamics in Peptides by Use of Temperature-Jump IR Spectroscopy and Isotope Labeling.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Major Factors for the Persistent Folding of Hybrid α, β, γ-Hybrid Peptides Into Hairpins.Frontiers in chemistry · 2020Article
- Modeling the mechanism of CLN025 beta-hairpin formation.The Journal of chemical physics · 2017Article
- Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly.Scientific reports · 2016Article
- Multiscale implementation of infinite-swap replica exchange molecular dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2016Review
- Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.The journal of physical chemistry. B · 2016Article
- 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
- How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014Article
- Aggregation gatekeeper and controlled assembly of Trpzip β-hairpins.Biochemistry · 2014Article
- Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.Journal of the American Chemical Society · 2014Article
- Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Journal of the American Chemical Society · 2013Article
- Combining coarse-grained protein models with replica-exchange all-atom molecular dynamics.International journal of molecular sciences · 2013Article
- Mutational effects on the folding dynamics of a minimized hairpin.Biochemistry · 2013Article
- Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.Scientific reports · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Both turn sequence and interstrand hydrophobic side-chain-side-chain interaction have been suggested to be important determinants of beta-hairpin stability. However, their roles in controlling the folding dynamics of beta-hairpins have not been clearly determined. Herein, we investigated the structural stability and folding kinetics of a series of tryptophan zippers by static IR and CD spectroscopies and the IR temperature jump method. Our results support a beta-hairpin folding mechanism wherein the rate-limiting event corresponds to the formation of the turn. We find that the logarithm of the folding rate depends linearly on the entropic change associated with the turn formation, where faster folding correlates with lower entropic cost. Moreover, a stronger turn-promoting sequence increases the stability of a beta-hairpin primarily by increasing its folding rate, whereas a stronger hydrophobic cluster increases the stability of a beta-hairpin primarily by decreasing its unfolding rate.
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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.