Zobrazeno 1 - 10
of 137
pro vyhledávání: '"free energy simulation"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
AlphaFold is a neural network–based tool for the prediction of 3D structures of proteins. In CASP14, a blind structure prediction challenge, it performed significantly better than other competitors, making it the best available structure prediction
Externí odkaz:
https://doaj.org/article/2421ecb4b8274e9a88038f742176b794
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 2526-2536 (2021)
Because of high stability and slow unfolding rates of G-quadruplexes (G4), cells have evolved specialized helicases that disrupt these non-canonical DNA and RNA structures in an ATP-dependent manner. One example is DHX36, a DEAH-box helicase, which p
Externí odkaz:
https://doaj.org/article/d2352cb5bece421bb065553b83cc5d1d
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Pyridoxal-5′-phosphate (PLP) is a cofactor in the reactions of over 160 enzymes, several of which are implicated in diseases. Methionine γ-lyase (MGL) is of interest as a therapeutic protein for cancer treatment. It binds PLP covalently through a
Externí odkaz:
https://doaj.org/article/56fadc36edce4ca6871917c893c55f21
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The grand challenge in structure-based drug design is achieving accurate prediction of binding free energies. Molecular dynamics (MD) simulations enable modeling of conformational changes critical to the binding process, leading to calculation of the
Externí odkaz:
https://doaj.org/article/2d57e19c0f43462492e0d19ae18cb8d3
Akademický článek
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Autor:
Qinfang Sun, Ronald M. Levy, Karen A. Kirby, Zhengqiang Wang, Stefan G. Sarafianos, Nanjie Deng
Publikováno v:
Viruses, Vol 13, Iss 5, p 920 (2021)
While drug resistance mutations can often be attributed to the loss of direct or solvent-mediated protein−ligand interactions in the drug-mutant complex, in this study we show that a resistance mutation for the picomolar HIV-1 capsid (CA)-targeting
Externí odkaz:
https://doaj.org/article/c8b17cfcdf6b46e4aa486a13d0012ca3
Publikováno v:
Frontiers in Molecular Biosciences, Vol 4 (2018)
The Molecular Mechanics Poisson-Boltzmann Surface Area (MMPBSA) approach has been widely applied as an efficient and reliable free energy simulation method to model molecular recognition, such as for protein-ligand binding interactions. In this revie
Externí odkaz:
https://doaj.org/article/b20434ef92aa4ef28370f99683978855
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 2526-2536 (2021)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
Graphical abstract
Because of high stability and slow unfolding rates of G-quadruplexes (G4), cells have evolved specialized helicases that disrupt these non-canonical DNA and RNA structures in an ATP-dependent manner. One example is DHX36, a DE
Because of high stability and slow unfolding rates of G-quadruplexes (G4), cells have evolved specialized helicases that disrupt these non-canonical DNA and RNA structures in an ATP-dependent manner. One example is DHX36, a DE
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f9c45ff14a9375a0e415c071dae6323
https://doi.org/10.1016/j.csbj.2021.04.039
https://doi.org/10.1016/j.csbj.2021.04.039
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
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Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, 2022, 9, pp.886358. ⟨10.3389/fmolb.2022.886358⟩
Frontiers in Molecular Biosciences, 2022, 9, pp.886358. ⟨10.3389/fmolb.2022.886358⟩
Pyridoxal-5′-phosphate (PLP) is a cofactor in the reactions of over 160 enzymes, several of which are implicated in diseases. Methionine γ-lyase (MGL) is of interest as a therapeutic protein for cancer treatment. It binds PLP covalently through a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ed726a08ebae84e817b3ab64aa61e36
https://hal-polytechnique.archives-ouvertes.fr/hal-03663983
https://hal-polytechnique.archives-ouvertes.fr/hal-03663983
