Change of mean residue ellipticity during the fast (A) and slow (B) phase of folding and unfolding (C) of wild-type (black) and Trp95Leu β2-m (blue). The kinetic traces were acquired at pH 7.4 and 30°C in the presence of 0.3 M and 5.1 M GdnHCl for folding and unfolding, respectively. Ellipticity at 215 nm was monitored for the fast phase of folding and unfolding, whereas change in 263 nm mean residue ellipticity was used in the slow phase of folding (B). Mean residue ellipticities at 215 nm of denatured protein (filled red circle), wild-type (empty black circle) and Trp95Leu β2-m (empty blue circle) are reported in (A) for comparison.
Raimondi et al. BMC Evolutionary Biology 2011 11:159 doi:10.1186/1471-2148-11-159