Heat-induced secondary structural studies of human serum albumin in aqueous solutions by two-dimensional FT-IR spectroscopy

Wu, Yuqing; Murayama, Koichi; Czarnik-Matusewicz, Boguslawa; Ozaki, Yukihiro
March 2000
AIP Conference Proceedings;2000, Vol. 503 Issue 1, p279
Academic Journal
FT-IR spectra were measured for human serum albumin (HSA) in aqueous solutions with the concentration of 1.0, 2.0, 3.0, 4.0 and 5.0 wt% over a temperature range of 45 to 80 °C. The synchronous and asynchronous correlation spectra were calculated for the concentration dependent IR spectral variation in the amide I and amide II regions at various temperatures. These result suggest that the thermal unfolding procedure begins with some changes in α-helix structure, followed by the conversion from the α-helix to β-strands and then to β-turn and disordered structures. The final state at higher temperatures is dominated by the β-turns and disordered structures. © 2000 American Institute of Physics.


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