Front Cover: Computational Insights into the Allosteric Effect and Dynamic Structural Features of the SARS‐COV‐2 Spike Protein (Chem. Eur. J. 6/2022)

Abstract

Although the prefusion conformation of the spike protein of SARS-COV-2 can be stabilized alone, a spontaneously and energy-friendly centripetal movement of the receptor binding domain occurs when spike protein binds to ACE2. During the binding process, several residues, especially Phe329 and Phe515, play a significant role in the allosteric effect. As a result, two potential cleavage sites S1/S2 and S2′ are exposed on the surface. More information can be found in the Research Article by A. Zhang, J. Fu et al. (DOI: 10.1002/chem.202104215).