Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2001 Aug;10(8):1685–1688. doi: 10.1110/ps.5101

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2001 The Protein Society

PMC Copyright notice

Fig. 3. — Refolding kinetics of wild-type cytochrome c₅₅₁ (filled circles), E70Q (open triangles), and E70V (open squares) mutants measured by fluorescence stopped-flow (Applied Photophysics SX18, Letherhead, UK) urea dilution experiments at pH 7.0 (phosphate buffer 50 mM) and 10°C in the presence of [GdnHCl] = 0.5 M. The lines are the best fit to the experimental data by using the equation

The ratio k_F^wt/k_F^mut obtained from the extrapolated values is approximately the same as that obtained in "classical" GdnHCl refolding experiments (see Table 2). This observation suggests that the E70–K10 salt bridge is already broken at 0.5 M GdnHCl.

graphic file with name M1.gif — Refolding kinetics of wild-type cytochrome c₅₅₁ (filled circles), E70Q (open triangles), and E70V (open squares) mutants measured by fluorescence stopped-flow (Applied Photophysics SX18, Letherhead, UK) urea dilution experiments at pH 7.0 (phosphate buffer 50 mM) and 10°C in the presence of [GdnHCl] = 0.5 M. The lines are the best fit to the experimental data by using the equation

The ratio k_F^wt/k_F^mut obtained from the extrapolated values is approximately the same as that obtained in "classical" GdnHCl refolding experiments (see Table 2). This observation suggests that the E70–K10 salt bridge is already broken at 0.5 M GdnHCl.