The University of Queensland, NCRIS Biotechnology Products, Australian Institute for Bioengineering and Nanotechnology, Brisbane QLD 4072, Australia.
Appl Spectrosc. 2010 Nov;64(11):1259-64. doi: 10.1366/000370210793335025.
Far-infrared (FIR) spectroscopy in the spectral region of 50-450 cm(-1) was used to study a series of protein higher-order structures constructed using β-lactoglobulin and polyomavirus capsid protein VP1. There were marked differences in the spectra for β-lactoglobulin monomer and dimer and between untreated β-lactoglobulin and heat-induced gels formed at neutral pH. Untreated β-lactoglobulin and heat-induced gels formed at acidic pH exhibited little difference in their spectra. Assembly of the quaternary structure of polyomavirus virus-like particles also caused large changes in the FIR spectra. These findings suggest that FIR spectroscopy may prove useful in studying some protein quaternary and higher-order structures. There was evidence of detection of β-lactoglobulin dimerization, intermolecular disulfide bonding in heat-induced neutral gels, and polyomavirus virus-like particle assembly but no evidence that FIR could detect β-lactoglobulin fibrils with their polymeric structure and hydrogen-bonded intermolecular β-pleated sheeting.
远红外（FIR）光谱在 50-450 cm(-1) 的光谱区域用于研究使用β-乳球蛋白和多瘤病毒衣壳蛋白 VP1 构建的一系列蛋白质高级结构。β-乳球蛋白单体和二聚体以及未经处理的β-乳球蛋白和在中性 pH 下形成的热诱导凝胶之间的光谱有明显差异。未经处理的β-乳球蛋白和在酸性 pH 下形成的热诱导凝胶的光谱几乎没有差异。多瘤病毒类病毒颗粒的四级结构组装也导致 FIR 光谱发生了很大变化。这些发现表明，FIR 光谱学可能在研究某些蛋白质四级和高级结构方面具有一定的应用价值。有证据表明可以检测到β-乳球蛋白二聚化、热诱导中性凝胶中的分子间二硫键以及多瘤病毒类病毒颗粒的组装，但没有证据表明 FIR 可以检测到具有聚合结构和氢键结合的分子间β-折叠片层的β-乳球蛋白纤维。
