English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The presence of the intermediate in the folding of ubiquitin is still under debate. Two distinct folding models have been proposed: two-state model and non-two state model involving the intermediates. To reveal each state hidden by the ensemble averaging in a conventional method, we investigated the folding dynamics of ubiquitin at a single molecule level by using a line confocal microscope coupled with a microfluidic tip. We used the mutant of ubiquitin labeled with two different dyes. More than 100 time series of the FRET efficiency were obtained at several GdnHCl concentrations. Our data clearly indicate that the folding intermediate whose FRET efficiency is located between the native and denatured states populates significantly at a moderate GdnHCl concentration.

2P061 Dynamics of ubiquitin folding detected by single molecule fluorescence spectroscopy(01C. Protein: Property)