Investigating the Structural Change in Protein Aqueous Solution using Temperature-Dependent Near-Infrared Spectroscopy and Continuous Wavelet Transform

The circulatory protein, human serum albumin (HSA), is widely used as a model protein for the study of protein structure. In this work, the structures of human serum albumin in aqueous solutions are studied using temperature-dependent near-infrared (NIR) spectroscopy with the aid of continuous wavelet transform (CWT). Near-infrared spectra of human serum albumin solutions with different concentrations were measured over a temperature range of 30–85 ℃. Then, continuous wavelet transform was performed on the spectra to enhance the resolution. As a result of the resolution enhancement, spectral bands around 4361, 4521, 4600 and 4260 cm−1 were extracted from the overlapping low-resolution signals. The four bands can be assigned to the protein structures of α-helix, β-sheet, an intermediate state and side chains, respectively. The variations in intensity of the bands around 4361 and 4521 cm−1 with temperature show that the increase of temperature leads to the loss of α-helical structure but the formation of β-...