Figure 2: IR spectral signature of albumin heating.
From: Anisotropic energy flow and allosteric ligand binding in albumin

(a) Equilibrium temperature dependent Fourier transform infrared (FTIR) difference spectra of 800 μM malachite green/BSA (MG/BSA) and metalloporphyrin/BSA (MP/BSA) (25–20 °C) with 300 ns transient IR amplitudes overlaid as magenta crosses (scaled to match ΔT of FTIR difference spectrum); (b) 800 ps TRIR spectrum of free MG (black) and the MG/BSA complex (red), obtained as an average of 2,000 laser pulses; (c) ns T-jump transients of the MG/BSA complex monitored at the indicated frequencies, showing the timescale for development of equilibrium difference features (average of 1,000 shots).