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. 2021 Mar 9;13(3):439. doi: 10.3390/v13030439

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Binding interactions and energy of spike proteins with C135 antibody. (A) The hydrogen bond peaks showing the interaction of mutants were better than wildtype spike protein. (B) The binding interaction of wildtype spike protein with heavy chain of C135 antibody, N501 (circled) making hydrophobic contact (hydrogen bonds are shown with green dots and non-polar interactions with magenta and brick semicircle). (C) The binding interaction of N501Y mutant spike protein with heavy chain of C135 antibody. (D) The binding interaction of N440K mutant spike protein with heavy chain of C135 antibody.