牛血清白蛋白
化学
变性(裂变材料)
水溶液
分析化学(期刊)
光谱学
红外光谱学
谱线
卵清蛋白
蛋白质结构
结晶学
色谱法
物理化学
生物化学
核化学
生物
量子力学
物理
有机化学
免疫系统
免疫学
天文
作者
Shiying Wang,Mian Wang,Li Han,Yan Sun,Wensheng Cai,Xueguang Shao
标识
DOI:10.1016/j.saa.2021.120581
摘要
To understand the stability of protein in confined environment, the near-infrared (NIR) spectra of aqueous solutions and reverse micelles (RMs) containing bovine serum albumin (BSA), human serum albumin (HSA) and ovalbumin (OVA) were measured at different temperature. With the resolution enhanced spectra calculated by continuous wavelet transform (CWT), the intensity change of the α-helix band at 4617 cm-1 with temperature shows a clear denaturation of the protein in aqueous solution but not in RMs. The effect of the confined environment on the stability of the proteins is indicated. More importantly, the intensity change of the spectral bands of water around 6956 and 6842 cm-1 provide an evidence for the denaturation, suggesting that water can be a probe exhibiting the structural change of proteins. Furthermore, comparing the spectral features of different water structures obtained by principal component analysis (PCA) from the spectra of RM with and without BSA, it is demonstrated that the bridging water connecting NH in protein and SO in the inner surface of RM may be the reason for the stabilization.
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