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.
Terahertz Biological Sensing Research Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
H
H
Yoneyama
M
M
Yamashita
S
S
Kasai
K
K
Kawase
R
R
Ueno
H
H
Ito
T
T
Ouchi
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