"Secondary structures of protein amide Ⅲ band and its thermal denaturation in natural rubber"

Abstract

Secondary structures of protein amide Ⅲ band and its thermal denaturation in natural rubber were studied by midinfrared (MIR) spectroscopy. The result of variable temperaturet deconvolution MIR spectroscopy showed that the infrared absorption peak intensity of irregular curled, β-folded, α-spiral and β-corner se-condary structures decreased when the temperature increased from 293 to 393 K. The result of two-dimensional MIR spectroscopy showed that there were significant differences in the sensitivity of amide Ⅲ band secondary structures to heat, with the irregular curled secondary structure being the first to change. Under thermal disturbance factor, the irregular curled secondary structure change was a key step in the overall secondary structure change of the amide Ⅲ band.

Keywords

• natural rubber， secondary structure of protein， amide ⅲ band， two-dimensional mid-infrared spectroscopy， thermal denaturation，