Abstract
The surface of proteins is vital in determining protein functions. Herein, a program, Protein Surface Printer (PSP), is built that performs multiple functions in quantifying protein surface domains. Two proteins, PETase and cytochrome P450, are used to validate that the program supports atomistic simulations with different combinations of programs and force fields. A case study is conducted on the structural analysis of the spike proteins of SARS-CoV-2 and SARS-CoV and the human cell receptor ACE2. Although the surface domains of both spike proteins are highly similar, their receptor-binding domains (RBDs) and the O-linked glycan domains are structurally different. The O-linked glycan domain of SARS-CoV-2 is highly positively charged, which may promote binding to negatively charged human cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5255-5264 |
| Number of pages | 10 |
| Journal | Journal of Chemical Information and Modeling |
| Volume | 60 |
| Issue number | 10 |
| DOIs | |
| State | Published - Oct 26 2020 |
Funding
This work was supported by the U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences, under Award No. DE-FG02-08ER46539, the Sherman Fairchild Foundation, and the Center for Computation and Theory of Soft Materials at Northwestern University.
ASJC Scopus subject areas
- General Chemistry
- General Chemical Engineering
- Computer Science Applications
- Library and Information Sciences
