scholarly journals Structure Model Analysis Of Phosphorylation Dependent Binding And Sequestration Of SARS-COV-2 Encoded Nucleocapsid Protein By Protein 14-3-3

2020 ◽  
Author(s):  
Pierre Limtung ◽  
H.Y. Lim Tung
Keyword(s):  
Binding Energy ◽  
Nucleocapsid Protein ◽  
Energy Difference ◽  
Model Analysis ◽  
Cellular Mechanism ◽  
Structure Model ◽  
Calculated Binding Energy ◽  
Binding Energy Difference ◽  
The Stability ◽  
Stability Energy

AbstractPhosphorylation of serines 197 and 206 of SARS-COV-2 Nucleocapsid protein (NCp) enhanced the stability and binding efficiency and sequestration of NCp to Protein 14-3-3 by increasing the Stability Energy (ΔGstability energy) and Binding Energy (ΔΔGbinding energy) from ~545 Kcal/mol to ~616 Kcal/mol, and from 108 Kcal/mol to ~228 Kcal/mol respectively. The calculated Binding Energy Difference (ΔΔGbinding energy difference) between dephospho-NCp-14-3-3 complex and phospho-NCp-13-3-3 complex was ~72 Kcal/mol. Phosphorylations of serines 186, 197, 202 and 206, and threonines 198 and 205 NCp also caused an increase in the Stability Energy (ΔGstability energy) and Binding Energy (ΔΔGbinding energy) from ~545 Kcal/mol to ~617, 616, 583, 580, 574, 564 and 566 Kcal/mol and from ~108 Kcal/mol to ~228, 216, 184, 188, 184, 174 and 112 Kcal/mol respectively. Phosphorylation of NCp on serines 197 and 206 caused a decrease in Stability Energy and Binding Energy from ~698 Kcal/mol to 688 Kcal/mol, and from ~91 Kcal/mol to ~82 Kcal/mol for the dimerization of NCp. These results support the existence of a phosphorylation dependent cellular mechanism to bind and sequester NCp.

Structure Model Analysis of the Effects of Mutations in the Phosphorylation Sites of SARS-CoV-2 Encoded Nucleocapsid Protein

2020 ◽  
Vol 3 (1) ◽  
pp. 023-030
Author(s):  
Pierre Limtung ◽  
HY Lim Tung
Keyword(s):  
Binding Energy ◽  
Nucleocapsid Protein ◽  
Thermodynamic Calculation ◽  
Model Analysis ◽  
Structure Modeling ◽  
Phosphorylation Sites ◽  
Structure Model ◽  
Rich Domain ◽  
Recognition Sites ◽  
Stability Energy

Mutations in several phosphorylation sites within the phosphorylation rich domain of SARS-COV-2 Nucleocapsid protein (NCp), including serines 186, 197 and 202, and adjacent arginine 203 and glycine 204 have been described and have been proposed to prevent the binding and sequestration of NCp by Protein 14-3-3. Structure modeling and thermodynamic calculation show that mutations of phosphorylation sites, phospho-serines 186, 197 and 202 to phenylalanine, leucine and asparagine, and phosphorylation recognition sites, arginine/glycine 203/204 to lysine/arginine or lysine/threonine resulted in signifi cant destabilization of the NCp-14-3-3 complex by causing a decrease in Stability Energy (ΔGstability energy) and Binding Energy (ΔΔGbinding energy). These results evidenced that mutations in NCp underlie a mechanism to bypass sequestration by Protein 14-3-3 which would result in enhanced dimerization of NCp, and replication, transcription and packaging of the SARS-COV-2 genome

Origin of the Ba core-level binding-energy difference between tetragonal and orthorhombicYBa2Cu3O7−δ

1991 ◽  
Vol 43 (4) ◽  
pp. 3695-3698 ◽  
Author(s):  
F. Parmigiani ◽  
G. Pacchioni ◽  
C. R. Brundle ◽  
D. E. Fowler ◽  
P. S. Bagus
Keyword(s):  
Binding Energy ◽  
Energy Difference ◽  
Core Level ◽  
Binding Energy Difference ◽  
Core Level Binding Energy

The Λ4HeΛ4H binding energy difference

1979 ◽  
Vol 83 (3-4) ◽  
pp. 289-292 ◽  
Author(s):  
B.F. Gibson ◽  
D.R. Lehman
Keyword(s):  
Binding Energy ◽  
Energy Difference ◽  
Binding Energy Difference

Nuclear charge symmetry breaking and the3H−3He binding energy difference

1988 ◽  
Vol 37 (2) ◽  
pp. 781-785 ◽  
Author(s):  
R. A. Brandenburg ◽  
G. S. Chulick ◽  
Y. E. Kim ◽  
D. J. Klepacki ◽  
R. Machleidt ◽  
...  
Keyword(s):  
Binding Energy ◽  
Symmetry Breaking ◽  
Nuclear Charge ◽  
Energy Difference ◽  
Charge Symmetry Breaking ◽  
Charge Symmetry ◽  
Binding Energy Difference
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