Author: David N. Frick; Rajdeep S. Virdi; Nemanja Vuksanovic; Narayan Dahal; Nicholas R Silvaggi
Title: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose Document date: 2020_4_2
ID: 02q9y011_8
Snippet: The energetics of ADP-ribose binding to the SARS-CoV protein are similar to those seen with the same protein from SARS-CoV-1, 9 MERS-CoV. 8 Enthalpy and entropy of binding were also very similar for all three protein (Fig. 3D ). Unlike what is seen with the macro X protein from an alpha coronavirus, 5 enthalpy appears to drive ADP-ribose binding to the macro X domains of the three beta coronaviruses......
Document: The energetics of ADP-ribose binding to the SARS-CoV protein are similar to those seen with the same protein from SARS-CoV-1, 9 MERS-CoV. 8 Enthalpy and entropy of binding were also very similar for all three protein (Fig. 3D ). Unlike what is seen with the macro X protein from an alpha coronavirus, 5 enthalpy appears to drive ADP-ribose binding to the macro X domains of the three beta coronaviruses.
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