Thermal denaturation of CP43 studied by Fourier transform-infrared spectroscopy and terahertz time-domain spectroscopy.
Thermal denaturation of CP43 was studied by Fourier transform-infrared (FT-IR) spectroscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and terahertz time-domain spectroscopy (THz-TDS). Under heat treatment, the secondary structure of CP43 changed, and the main thermal transition occurred at 59 degrees C. During the process, CP43 aggregated at first, and then with increasing temperature degraded. The low-frequency collective vibrational modes of CP43 changed with increasing temperature and decreasing mass. THz-TDS is a new technique used to study the conformational state of a molecule, and it is the first use of this technique to study the photosynthesis membrane proteins in this paper. The results presented here demonstrate that THz-TDS has both advantages and disadvantages in monitoring the thermal denaturation of membrane proteins, which is important in applying THz-TDS technique to study of biomolecules.
Qu
Yuangang
Y
Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Institute of Botany, The Chinese Academy of Sciences, No. 20, Nanxincun, Xiangshan, Haidian District, Beijing 100093, China.
Chen
Hua
H
Qin
Xiaochun
X
Li
Liangbi
L
Wang
Li
L
Kuang
Tingyun
T
D011232:Chemical Precipitation; D006358:Hot Temperature; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D045332:Photosystem II Protein Complex / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D011846:Radio Waves; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis / Q000379:methods*; D018724:Spinacia oleracea / Q000737:chemistry
D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; C083100:photosystem II, chlorophyll binding protein, CP-43