generalized born with switching function (gbsw) implicit solvent model (Molecular Dynamics Inc)
90
Structured Review
Molecular Dynamics Inc
generalized born with switching function (gbsw) implicit solvent model
Generalized Born With Switching Function (Gbsw) Implicit Solvent Model, 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/product/generalized+born+with+switching+function+(gbsw)+implicit+solvent+model/generalized+born+with+switching+function++gbsw++implicit+solvent+model/pm16475196-59-5-39
Average 90 stars, based on 1 article reviews
Generalized Born With Switching Function (Gbsw) Implicit Solvent Model, 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/product/generalized+born+with+switching+function+(gbsw)+implicit+solvent+model/generalized+born+with+switching+function++gbsw++implicit+solvent+model/pm16475196-59-5-39
Average 90 stars, based on 1 article reviews
generalized born with switching function (gbsw) implicit solvent model - by Bioz Stars,
2026-09
90/100 stars
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Solvent:Article Title: Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Article Snippet: A combination of thirty-two 10-nsscale molecular dynamics simulations were used to explore the coupling between conformational transition and phosphorylation in the bacteria chemotaxis Y protein (CheY), as a simple but representative example of protein allostery.. Results from these simulations support an activation mechanism in which the 4– 4 loop, at least partially, gates the isomerization of Tyr106.. The roles of phosphorylation and the conserved Thr87 are deemed indirect in that they stabilize the active configuration of the 4– 4 loop. Residue:Article Title: Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Article Snippet: A combination of thirty-two 10-nsscale molecular dynamics simulations were used to explore the coupling between conformational transition and phosphorylation in the bacteria chemotaxis Y protein (CheY), as a simple but representative example of protein allostery.. Results from these simulations support an activation mechanism in which the 4– 4 loop, at least partially, gates the isomerization of Tyr106.. The roles of phosphorylation and the conserved Thr87 are deemed indirect in that they stabilize the active configuration of the 4– 4 loop. Mutagenesis:Article Title: Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Article Snippet: A combination of thirty-two 10-nsscale molecular dynamics simulations were used to explore the coupling between conformational transition and phosphorylation in the bacteria chemotaxis Y protein (CheY), as a simple but representative example of protein allostery.. Results from these simulations support an activation mechanism in which the 4– 4 loop, at least partially, gates the isomerization of Tyr106.. The roles of phosphorylation and the conserved Thr87 are deemed indirect in that they stabilize the active configuration of the 4– 4 loop. Modification:Article Title: Reconciling the "old" and "new" views of protein allostery: a molecular simulation study of chemotaxis Y protein (CheY). Article Snippet: A combination of thirty-two 10-nsscale molecular dynamics simulations were used to explore the coupling between conformational transition and phosphorylation in the bacteria chemotaxis Y protein (CheY), as a simple but representative example of protein allostery.. Results from these simulations support an activation mechanism in which the 4– 4 loop, at least partially, gates the isomerization of Tyr106.. The roles of phosphorylation and the conserved Thr87 are deemed indirect in that they stabilize the active configuration of the 4– 4 loop. |