Figure 7: Comparison of the aggregation behaviour of WT and mutant PA.
From: Structural hot spots for the solubility of globular proteins
(a) The hydrodynamic radius (RH) of WT and single Gk mutant PA before (green bar) and after exposure (red bar) to thermal stress at 45 °C for 30 min. (b) Infrared amide I band of the WT (NATNIYTVLDKIK) and mutant sequence (NATNIYEVLDKIK) surrounding the mutation site of PA APR 1. (c) Western blot of WT, single and double mutant PA before and after exposing to thermal stress at 45 °C for 30 min. The lanes 1 and 2 of each sample represent the soluble fraction of PA under normal conditions (25 °C) and after thermal heat stress (40 °C for 30 min). (d) Far UV circular dichroism (CD) spectra of the WT and double-mutant (T576E/S559L) PA at 25 °C. (e) DSC thermogram of WT (red) and double-mutant (T576E/S559L) PA (green). (f) Static light scattering (SLS) at 473 nm measured over time for WT (red) and double-mutant (T576E/S559L) (green) at 40 °C.
