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S-265C and S-126/265C ESBL populate intermediate states unfolded by fluorescence and thiol reactivity but with full secondary structure.
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Such an alteration was associated with a new conformational state (unfolded state) [45].
We observed the state (unfolded state) where α-helix of the immobilized enzyme is lower than that of the free one.
We explore the free energy landscape of the native state, the unfolded state, and possible intermediates, with replica exchange molecular dynamics.
We find that the free energy landscape has the desired shape (i.e. stable native state, unstable unfolded state) at temperatures below 0.5, as shown in Figure 3.
Results showed that GdnHCl-induced unfolding of apoNgb is a three-state pathway through an intermediate state, Native state (N) → Intermediate state (I)→ Unfolded state (U).
The folded state, the transition state, and the unfolded state are located at positions of 0, 1/3, and 1 in the unit of total extension change of CTD transition.
The GdnHCl-induced unfolding of apoNgb can be described as the following scheme: (1) Native state (N ) → Intermediate state (I ) → Unfolded state (U ).
At higher charge states, an unfolded population of PagP is observed, likely due to gas phase unfolding.
Chemical chaperones are small organic compounds which favor compact protein states over unfolded states through the so-called "solvophobic effect", which involves destabilizing interactions of the water/chaperone mixture with the polypeptide backbone [ 95].
These domains are enriched for asparagine, glutamine, tyrosine and glycine residues and can adopt two conformational states: an unfolded and an aggregated state.
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