Front Cover: Computational Insights into the Allosteric Effect and Dynamic Structural Features of the SARS‐COV‐2 Spike Protein (Chem. Eur. J. 6/2022)
Chemistry (Weinheim an der Bergstrasse, Germany)
; 28(6), 2022.
Article
in English
| EuropePMC | ID: covidwho-1801097
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).
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Collection:
Databases of international organizations
Database:
EuropePMC
Type of study:
Experimental Studies
Language:
English
Journal:
Chemistry (Weinheim an der Bergstrasse, Germany)
Year:
2022
Document Type:
Article
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