AI Article Synopsis

  • The Trp-cage miniprotein is a small protein that shows stable secondary structures and fast folding, making it ideal for studying temporary structures during the folding process.
  • Previous studies suggested that there is a single stable intermediate state in the Trp-cage folding pathway, which this research seeks to clarify using advanced methods.
  • By employing time-resolved X-ray solution scattering, the study found that the Trp-cage forms a stretched intermediate at 1 μs and completely unfolds by 5 μs, providing valuable insights for enhancing theoretical models of protein folding.

Article Abstract

The Trp-cage miniprotein is one of the smallest systems to exhibit a stable secondary structure and fast-folding dynamics, serving as an apt model system to study transient intermediates with both experimental and computational analyses. Previous spectroscopic characterizations that have been done on Trp-cage have inferred a single stable intermediate on a pathway from folded to unfolded basins. We aim to bridge the understanding of Trp-cage structural folding dynamics on microsecond-time scales, by utilizing time-resolved X-ray solution scattering to probe the temperature-induced unfolding pathway. Our results indicate the formation of a conformationally extended intermediate on the time scale of 1 μs, which undergoes complete unfolding within 5 μs. We further investigated the atomistic structural details of the unfolding pathway using a genetic algorithm to generate ensemble model fits to the scattering profiles. This analysis paves the way for direct benchmarking of theoretical models of protein folding ensembles produced with molecular dynamics simulations.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10167713PMC
http://dx.doi.org/10.1021/acs.jpclett.2c03680DOI Listing

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