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. 2007 Mar;12(1):20–32. doi: 10.1379/CSC-219R.1

Fig 4.

Fig 4.

The native state is stabilized for tsf:F170L coat proteins. Temperature shift experiments were performed as described in the Materials and Methods. In brief, natively folded coat protein held on ice was transferred to 33°C for 0–30 minutes. Samples were run on native polyacrylamide gels and silver stained to detect the presence of native monomers and aggregated forms. (A) Densitometry data taken from the native gels. The native fraction remaining is the intensity of the native band at the experimental time divided by the intensity at time 0. The lines drawn do not reflect a fit of the data to any model; they are drawn to aid the eye. Closed squares are data for WT coat protein; open circles are tsf coat protein; closed circles are tsf:F170L coat proteins. (B) The average fraction of native protein remaining after 30 minutes at 33°C; error bars are the standard deviation taken from 5 data sets