Comparing Terahertz transmission response on pH-dependent apomyoglobin proteins dynamics with circular dichroism

Terahertz time domain spectroscopy (THz-TDS) was used to study the transmission responses of pH-dependent apomyoglobin (ApoMb) dissolved solutions in 0.2-2.2 THz frequency domain, the THz-TDS technique was also benchmarked against circular dichroism (CD) by studying pH-related folding states changes of ApoMb protein. Results revealed that differences of pH-dependent ApoMb/water dynamics can be detected directly by the THz refractive index spectrum, and these differences are further proved to be caused mainly the effect of protonation of water and possibly water response leaded by protein conformation change.