Open AccessA Hydrophobic‐Interaction‐Based Mechanism Triggers Docking between the SARS‐CoV‐2 Spike and Angiotensin‐Converting Enzyme 2 (Global Challenges 12/2020)
Author(s) -
Li Jiacheng,
Ma Xiaoliang,
Guo Shuai,
Hou Chengyu,
Shi Liping,
Zhang Hongchi,
Zheng Bing,
Liao Chenchen,
Yang Lin,
Ye Lin,
He Xiaodong
Publication year - 2020
Publication title -
global challenges
Language(s) - English
Resource type - Journals
ISSN - 2056-6646
DOI - 10.1002/gch2.202070121
Subject(s) - docking (animal) , angiotensin converting enzyme 2 , spike (software development) , mechanism (biology) , chemistry , covid-19 , enzyme , spike protein , computational biology , computer science , biophysics , biology , biochemistry , medicine , physics , nursing , disease , software engineering , pathology , infectious disease (medical specialty) , quantum mechanics
In article number 2000067 Lin Yang and co‐workers find that the hydrophobic interaction between the SARS‐CoV‐2 spike protein and the ACE2 protein is significantly greater than that between the SARS‐CoV spike protein and the ACE2 protein. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS‐CoV‐2 S are found to be involved in the hydrophobic interaction between the SARS‐CoV‐2 spike protein and ACE2.