journal menu
![[Figure 3]](gm5080fig3mag.jpg)
|
|
Figure 3
DLS measurements of the v-Src SH3 variants. (a) v-Src SH3 W95R-I96T at 5 mg ml−1 in 50 mM sodium acetate buffer pH 5.0 in the absence (red line) and in the presence (black line) of 5% PEG 300 at 25°C. In the absence of PEG, the protein is a monomer with Rh = 1.8 ± 0.3 nm. After adding 5% PEG 300, the hydrodynamic radius increases to a value of 2.4 ± 0.5 nm. (b) Temperature-dependent aggregation of the v-Src SH3 N117D-V124L variant. After incubation for 24 h at three different temperatures, the protein was measured at 5 mg ml−1 in 50 mM sodium phosphate buffer pH 7.0. At low temperature (≤15°C) 99.9% of the protein is a monomer with an Rh of 1.8 ± 0.4 nm. At higher temperatures, the protein aggregates, forming high-molecular-weight oligomers, and after one day of incubation the monomer population decreases at both 20°C (66%) and 25°C (39%). These oligomers tested positive for amyloid aggregates using the ThT and CR assays. |
![[Figure 3]](gm5080fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
