Structure Model Analysis on Visitors Satisfaction of Sightseeing in Mt. Keumwon Arboretum

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

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Hierarchical Physical Competence Structure in Physical Education Class: Scale Validation and Structure Model Analysis

Korean Journal of Sport Science ◽

10.24985/kjss.2008.19.2.91 ◽

2008 ◽

Vol 19 (2) ◽

pp. 91-103 ◽

Cited By ~ 2

Author(s):

류민정

Keyword(s):

Physical Education ◽

Scale Validation ◽

Model Analysis ◽

Structure Model ◽

Physical Education Class ◽

Physical Competence ◽

Education Class ◽

Competence Structure

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

10.1101/2020.09.16.299362 ◽

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.

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Fast calibration of CBED patterns for quantitative analysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100149209 ◽

1993 ◽

Vol 51 ◽

pp. 674-675

Author(s):

M.A. Gribelyuk ◽

M. Rühle

Keyword(s):

Reciprocal Lattice ◽

Accurate Determination ◽

Incident Beam ◽

Crystal Thickness ◽

Structure Model ◽

Beam Direction ◽

Transmitted Beam ◽

Reciprocal Vector ◽

On Line

A new method is suggested for the accurate determination of the incident beam direction K, crystal thickness t and the coordinates of the basic reciprocal lattice vectors V1 and V2 (Fig. 1) of the ZOLZ plans in pixels of the digitized 2-D CBED pattern. For a given structure model and some estimated values Vest and Kest of some point O in the CBED pattern a set of line scans AkBk is chosen so that all the scans are located within CBED disks.The points on line scans AkBk are conjugate to those on A0B0 since they are shifted by the reciprocal vector gk with respect to each other. As many conjugate scans are considered as CBED disks fall into the energy filtered region of the experimental pattern. Electron intensities of the transmitted beam I0 and diffracted beams Igk for all points on conjugate scans are found as a function of crystal thickness t on the basis of the full dynamical calculation.

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