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.
Yoneyama
H
H
Terahertz Biological Sensing Research Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
Yamashita
M
M
Kasai
S
S
Kawase
K
K
Ueno
R
R
Ito
H
H
Ouchi
T
T
D008855:Microscopy, Electron, Scanning / Q000379:methods; D008872:Microwaves; D008968:Molecular Conformation; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine / Q000032:analysis* / Q000737:chemistry; D013057:Spectrum Analysis / Q000295:instrumentation / Q000379:methods*; D013696:Temperature; D013997:Time Factors
D012710:Serum Albumin, Bovine