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Toward quantitative estimates of binding affinities for protein-ligand systems involving large inhibitor compounds: A steered molecular dynamics simulation route

Autor
Nicolini, P.; Frezzato, D.; Gellini, C.; Bizzarri, M.; Chelli, R.
Tipus d'activitat
Article en revista
Revista
Journal of computational chemistry
Data de publicació
2013-07
Volum
34
Número
8
Pàgina inicial
1561
Pàgina final
1576
DOI
https://doi.org/10.1002/jcc.23286 Obrir en finestra nova
Repositori
http://hdl.handle.net/2117/19998 Obrir en finestra nova
URL
http://onlinelibrary.wiley.com/doi/10.1002/jcc.23286/abstract;jsessionid=A03A2970BEA21123571F02B6ED66E329.d04t03 Obrir en finestra nova
Resum
Understanding binding mechanisms between enzymes and potential inhibitors and quantifying protein–ligand affinities in terms of binding free energy is of primary importance in drug design studies. In this respect, several approaches based on molecular dynamics simulations, often combined with docking techniques, have been exploited to investigate the physicochemical properties of complexes of pharmaceutical interest. Even if the geometric properties of a modeled protein–ligand complex can be...
Citació
Nicolini, P. [et al.]. Toward quantitative estimates of binding affinities for protein-ligand systems involving large inhibitor compounds: A steered molecular dynamics simulation route. "Journal of computational chemistry", Juliol 2013, vol. 34, núm. 8, p. 1561-1576.
Paraules clau
Binding Free Energy, Protein–ligand Complexes, Steered Molecular Dynamics Simulations, Focal Adhesion Kinase

Participants

  • Nicolini, Paolo  (autor)
  • Frezzato, Diego  (autor)
  • Gellini, Cristina  (autor)
  • Bizzarri, Marco  (autor)
  • Chelli, Riccardo  (autor)