Journal
CHEMICAL SCIENCE
Volume 12, Issue 9, Pages 3282-3289Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0sc06106a
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Funding
- National Natural Science Foundation of China [22027806, 22090051, 21922405]
- Excellent Research Program of Nanjing University [ZYJH004]
- Fundamental Research Funds for the Central Universities [14380239]
- Open Research Fund of State Key Laboratory of Bioelectronics, Southeast University
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The use of solid-state nanopores with electrochemical confinement allowed for the capture of transient conformations of proteins and tracking of multiple transition pathways of single peptides. The new single-molecule technique, combined with a Markov chain model, clarified non-equilibrium fluctuations in the transition pathways of the beta-hairpin peptide. This method provides high-throughput investigation of transition pathways, offering insights into protein folding mechanisms.
A fundamental question relating to protein folding/unfolding is the time evolution of the folding of a protein into its precisely defined native structure. The proper identification of transition conformations is essential for accurately describing the dynamic protein folding/unfolding pathways. Owing to the rapid transitions and sub-nm conformation differences involved, the acquisition of the transient conformations and dynamics of proteins is difficult due to limited instrumental resolution. Using the electrochemical confinement effect of a solid-state nanopore, we were able to snapshot the transient conformations and trace the multiple transition pathways of a single peptide inside a nanopore. By combining the results with a Markov chain model, this new single-molecule technique is applied to clarify the transition pathways of the beta-hairpin peptide, which shows nonequilibrium fluctuations among several blockage current stages. This method enables the high-throughput investigation of transition pathways experimentally to access previously obscure peptide dynamics, which is significant for understanding the folding/unfolding mechanisms and misfolding of peptides or proteins.
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