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Front Cover: Computational Insights into the Allosteric Effect and Dynamic Structural Features of the SARS‐COV‐2 Spike Protein (Chem. Eur. J. 6/2022)
Author(s) -
Xue Qiao,
Liu Xian,
Pan Wenxiao,
Zhang Aiqian,
Fu Jianjie,
Jiang Guibin
Publication year - 2022
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202200157
Subject(s) - allosteric regulation , spike (software development) , spike protein , biophysics , front cover , covid-19 , chemistry , energy landscape , binding domain , cleavage (geology) , molecular dynamics , cover (algebra) , receptor , binding site , biology , biochemistry , computer science , computational chemistry , medicine , infectious disease (medical specialty) , software engineering , disease , pathology , mechanical engineering , paleontology , fracture (geology) , engineering
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).