Fig. 1.

UVCD spectroscopic analysis of the effect of heat on the structure of human desmin (A), human GFAP (B), and rabbit muscle actin (C). The far UVCD spectra of desmin, GFAP, and actin were measured at 23°C and after heating at 45°C for 15mins, which was identical to the conditions used in the pin array assays. In the desmin spectrum, the negative ellipticity at 222nm increased from -4467 deg.cm².dmol^-1 at 23°C to -24677 deg.cm².dmol^-1 at 45°C indicating a gain of helical secondary structure with temperature which was consistent with previous reports (Fuchs & Weber, 1994). In the GFAP spectrum, the negative ellipticity at 222nm increased from -8596 deg.cm².dmol^-1 at 23°C to -11230 deg.cm².dmol^-1 at 45°C indicating a gain in helical secondary structure with temperature which was consistent with previous reports (Fuchs & Weber, 1994). Actin was thermostable up to 45°C, and the negative ellipticity at 222nm decreased from -2787 deg.cm².dmol^-1 at 23°C to -2753 deg.cm².dmol^-1 at 45°C, which was consistent with previous reports (Bertazzon, Tian, Lamblin, & Tsong, 1990; Bertazzon & Tsong, 1990). Based on UVCD, desmin and GFAP were determined to have more helical content at 45°C than at 23°C, while actin had slightly lower helical content at 45°C than at 23°C.