2018 simulation Search Results


finite element code abaqus 2018  (Abaqus Inc)
90
Abaqus Inc finite element code abaqus 2018
Finite Element Code Abaqus 2018, supplied by Abaqus Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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simulation 2018 software  (SolidWorks Corp)
90
SolidWorks Corp simulation 2018 software
Simulation 2018 Software, supplied by SolidWorks Corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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solidworks 2018 plastic flow simulator  (Dassault Systemes)
90
Dassault Systemes solidworks 2018 plastic flow simulator
Solidworks 2018 Plastic Flow Simulator, supplied by Dassault Systemes, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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md simulation biovia discovery studio 2018  (Accelrys)
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Accelrys md simulation biovia discovery studio 2018
Md Simulation Biovia Discovery Studio 2018, supplied by Accelrys, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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simulation interactions diagram module in desmond 2018-4  (GraphPad Software Inc)
90
GraphPad Software Inc simulation interactions diagram module in desmond 2018-4
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Simulation Interactions Diagram Module In Desmond 2018 4, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
simulation interactions diagram module in desmond 2018-4 - by Bioz Stars, 2026-04
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simulation engine gromacs-2018.3  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc simulation engine gromacs-2018.3
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Simulation Engine Gromacs 2018.3, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/simulation engine gromacs-2018.3/product/Molecular Dynamics Inc
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finite element modeling hfss ansys electronics desktop 2021 r1  (ANSYS inc)
90
ANSYS inc finite element modeling hfss ansys electronics desktop 2021 r1
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Finite Element Modeling Hfss Ansys Electronics Desktop 2021 R1, supplied by ANSYS inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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optical uniblitz ent and simulation of partially-premixed cellular (2018)  (Vincent Associates)
90
Vincent Associates optical uniblitz ent and simulation of partially-premixed cellular (2018)
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Optical Uniblitz Ent And Simulation Of Partially Premixed Cellular (2018), supplied by Vincent Associates, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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integrated simulator vivado 2018.2 design suite  (Xilinx Inc)
90
Xilinx Inc integrated simulator vivado 2018.2 design suite
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Integrated Simulator Vivado 2018.2 Design Suite, supplied by Xilinx Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/integrated simulator vivado 2018.2 design suite/product/Xilinx Inc
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process simulation cup 2018 v5.01  (Chemstations Europe GmbH)
90
Chemstations Europe GmbH process simulation cup 2018 v5.01
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Process Simulation Cup 2018 V5.01, supplied by Chemstations Europe GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/process simulation cup 2018 v5.01/product/Chemstations Europe GmbH
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simulation module of the biovia discovery studio 2018  (Accelrys)
90
Accelrys simulation module of the biovia discovery studio 2018
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Simulation Module Of The Biovia Discovery Studio 2018, supplied by Accelrys, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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amber 2018.10 simulation package  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc amber 2018.10 simulation package
2D <t>interactions</t> <t>diagram</t> of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization <t>module</t> in Maestro 2021.4 [ , ].
Amber 2018.10 Simulation Package, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


2D interactions diagram of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization module in Maestro 2021.4 [ , ].

Journal: Molecules

Article Title: Binding and Dynamics Demonstrate the Destabilization of Ligand Binding for the S688Y Mutation in the NMDA Receptor GluN1 Subunit

doi: 10.3390/molecules28104108

Figure Lengend Snippet: 2D interactions diagram of ligands bound to GluN1 LBD. Hydrophobic residues are shown in green, polar residues are shown in cyan, positively charged residues are shown in purple, and negatively charged residues are shown in orange. Hydrogen bonds are shown as purple arrows, π-cation interactions are shown as red lines, and salt bridges are shown as red-blue lines. The tip of the tear-drop shape points towards the side chain of the residue; dots on a connection indicate a residue not making contact with the ligand. ( A ) Glycine bound to the wild-type GluN1 LBD ( B ) D-serine bound to the wild-type GluN1 LBD. ( C ) Glycine bound to the S688Y GluN1 LBD ( D ) D-serine bound to the S688Y GluN1 LBD. Figure generated using the ligand interaction visualization module in Maestro 2021.4 [ , ].

Article Snippet: Graphs were generated using the Simulation Interactions Diagram module in Desmond 2018-4 [ , ] and GraphPad Prism version 9.5.0 for MacOS, GraphPad Software, San Diego, CA, USA.

Techniques: Residue, Generated

Averaged triplicate GluN1 LBD-ligand interactions of the 1 µs simulations. Note that figure scales are different to improve the visibility of the data. Hydrogen bonds are defined as an H-Acceptor distance less than 2.8 Å and a Donor-H-Acceptor angle greater than 120. Hydrophobic interactions include pi-pi stacking, pi-cation interactions, and van der Waals interactions within 3.6 Å of ligand. Ionic interactions are defined as charged interactions within 3.6 Å of the ligand. Water bridges are defined as H-Acceptor distances less than 2.7 Å. Hydrogen bonds are shown in green, hydrophobic interactions are shown in lilac, ionic interactions are shown in magenta, and water bridges are shown in blue. For residues with more than one type of interaction, the interaction fraction can exceed 1. ( A ) Glycine bound to wild-type GluN1 LBD, ( B ) D-serine bound to wild-type GluN1 LBD, ( C ) Glycine bound to S688Y GluN1 LBD, ( D ) D-serine bound to S688Y GluN1 LBD. Graphs were generated using the Simulation Interactions Diagram module of Maestro 2021.4 [ , ].

Journal: Molecules

Article Title: Binding and Dynamics Demonstrate the Destabilization of Ligand Binding for the S688Y Mutation in the NMDA Receptor GluN1 Subunit

doi: 10.3390/molecules28104108

Figure Lengend Snippet: Averaged triplicate GluN1 LBD-ligand interactions of the 1 µs simulations. Note that figure scales are different to improve the visibility of the data. Hydrogen bonds are defined as an H-Acceptor distance less than 2.8 Å and a Donor-H-Acceptor angle greater than 120. Hydrophobic interactions include pi-pi stacking, pi-cation interactions, and van der Waals interactions within 3.6 Å of ligand. Ionic interactions are defined as charged interactions within 3.6 Å of the ligand. Water bridges are defined as H-Acceptor distances less than 2.7 Å. Hydrogen bonds are shown in green, hydrophobic interactions are shown in lilac, ionic interactions are shown in magenta, and water bridges are shown in blue. For residues with more than one type of interaction, the interaction fraction can exceed 1. ( A ) Glycine bound to wild-type GluN1 LBD, ( B ) D-serine bound to wild-type GluN1 LBD, ( C ) Glycine bound to S688Y GluN1 LBD, ( D ) D-serine bound to S688Y GluN1 LBD. Graphs were generated using the Simulation Interactions Diagram module of Maestro 2021.4 [ , ].

Article Snippet: Graphs were generated using the Simulation Interactions Diagram module in Desmond 2018-4 [ , ] and GraphPad Prism version 9.5.0 for MacOS, GraphPad Software, San Diego, CA, USA.

Techniques: Generated