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. 2020 Nov 6;3(6):1111–1143. doi: 10.1021/acsptsci.0c00089

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© 2020 American Chemical Society

This article is made available via the ACS COVID-19 subset for unrestricted RESEARCH re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.

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Stereo views of the WATMD-calculated solvation structure within the dimerization interface of M_2/up^pro (2Q6G) with the NTLs of both subunits highlighted in yellow. (A) ULOVs and HOVs surrounding subunit A (pink), together with the overlapping regions of subunit B (gray). The corresponding H-bond depleted solvation is mutually expelled by subunits A and B during dimerization. Few overlaps exist between subunit B and the HOVs of subunit A. (B) Dimer interface in postdimerized apo M_2/up (6M03). Residual H-bond depleted solvation in the interface is counterbalanced by H-bond enriched solvation that is absent in the monomeric form of the protein.