Abstract：
Spike (S) glycoprotein is the largest structural protein of SARS-CoV-2 virus and the main one involved in anchoring of the host receptor ACE2 through the receptor binding domain (RBD). S protein secondary structure is of great interest for shedding light on various aspects, from functionality to pathogenesis, finally to spectral fingerprint for the design of optical biosensors. In this paper, the secondary structure of SARS-CoV-2 S protein and its constituting components, namely RBD, S1 and S2 regions, are investigated at serological pH by measuring their amide I infrared absorption bands through Attenuated Total Reflection Infrared (ATR-IR) spectroscopy. Experimental data in combination with MultiFOLD predictions, Define Secondary Structure of Proteins (DSSP) web server and Gravy value calculations, provide a comprehensive understanding of RBD, S1, S2, and S proteins in terms of their secondary structure content, conformational order, and interaction with the solvent.
摘要：
Spike（S）糖蛋白是SARS-CoV-2病毒的最大结构蛋白，也是通过受体结合域（RBD）参与宿主受体ACE2锚定的主要蛋白。S蛋白二级结构对于在各个方面发光非常感兴趣，从功能到发病机制，最后以光谱指纹进行光学生物传感器的设计。在本文中,SARS-CoV-2S蛋白及其组成成分的二级结构,即RBD,S1和S2区域，通过衰减全反射红外（ATR-IR）光谱法测量其酰胺I红外吸收带，在血清学pH下进行了研究。实验数据与MultiFOLD预测相结合，定义蛋白质的二级结构（DSSP）Web服务器和Gravy值计算，提供对RBD的全面了解，S1，S2和S蛋白的二级结构含量，构象顺序，以及与溶剂的相互作用。
