Terahertz spectroscopy of native-conformation and thermally denatured bovine serum albumin (BSA).

Proteins are expected to exhibit collective vibrational modes at terahertz frequencies. We have developed a promising approach to measure these motions by using a membrane device to hold samples. Samples of bovine serum albumin (BSA) in native and thermally denatured conformations were measured using terahertz time-domain spectroscopy. Clear differences were observed in transmittance and phase between native-conformation BSA samples and thermally denatured BSA samples. Time-domain data shows that samples exhibited relative time shifts when compared with a standard. Results suggest that there were differences in dielectric responses in the BSA samples, and these are probably associated with molecular conformational changes in the membrane device.