Skip to main content
. 1997 Dec 9;94(25):13932–13937. doi: 10.1073/pnas.94.25.13932

Figure 1.

Figure 1

Specificity of CD spectral shifts with Hsp104 and Sup35. (Right) Predicted (−−) and actual (—) spectra of mixed proteins. (Left) Individual spectra used to generate predicted spectra. (A) Sup35 in LSB1 (low salt buffer) with aldolase or Hsp70. (B) Hsp104 and aldolase or IgM in LSB1. (C) Hsp104 and Sup35 in LSB1 (Upper) and Hsp104 and Sup35 in HSB (Lower). Data, buffer spectra subtracted, are presented in millidegrees because the possibility of proteins partitioning out of solution invalidates molar ellipticity calculations. Hsp104, Hsp70, aldolase, or the buffer in which they were prepared was directly added to Sup35 at an ≈1:2.5 gram/weight ratio. Reactions were incubated for 1 hr with 1 mM ATP at 37°C, and spectra were then recorded at 25°C.