The Molecular Mechanism of Domain Swapping of the C-Terminal Domain of the SARS-Coronavirus Main Protease
- 24 December 2020
- journal article
- research article
- Published by Elsevier BV in Biophysical Journal
- Vol. 120 (3), 504-516
- https://doi.org/10.1016/j.bpj.2020.11.2277
Abstract
No abstract availableFunding Information
- Simons Foundation
- Department of Atomic Energy, Government of India
- Science and Engineering Research Board
This publication has 88 references indexed in Scilit:
- Mutation of Asn28 Disrupts the Dimerization and Enzymatic Activity of SARS 3CLpro,Biochemistry, 2010
- Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteinsProceedings of the National Academy of Sciences of the United States of America, 2010
- C‐terminal domain of SARS‐CoV main protease can form a 3D domain‐swapped dimerProtein Science, 2009
- Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kineticsProceedings of the National Academy of Sciences of the United States of America, 2009
- An all‐atom structure‐based potential for proteins: Bridging minimal models with all‐atom empirical forcefieldsProteins, 2008
- Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingProceedings of the National Academy of Sciences of the United States of America, 2008
- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular SimulationJournal of Chemical Theory and Computation, 2008
- Coarse-grained Models for Simulations of Multiprotein Complexes: Application to Ubiquitin BindingJournal of Molecular Biology, 2008
- Domain-swapped dimerization of the HIV-1 capsid C-terminal domainProceedings of the National Academy of Sciences of the United States of America, 2007
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996