蛋白质二级结构
蛋白质结构
生物物理学
病毒蛋白
糖蛋白
化学
红外光谱学
蛋白质三级结构
光谱学
生物
结晶学
病毒
病毒学
生物化学
物理
有机化学
量子力学
作者
Tiziana Mancini,Salvatore Macis,Rosanna Mosetti,Nicole Luchetti,Velia Minicozzi,A. Notargiacomo,Marialilia Pea,A. Marcelli,Giancarlο Della Ventura,S. Lupi,Annalisa D’Arco
标识
DOI:10.1002/advs.202400823
摘要
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.
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