Investigating the dynamic aspects of drug-protein recognition through a combination of MD and NMR analyses: implications for the development of protein-protein interaction inhibitors.
In this paper, we investigate the dynamic aspects of the molecular recognition between a small molecule ligand and a flat, exposed protein surface, representing a typical target in the development of protein-protein interaction inhibitors. Specifically, we analyze the complex between the protein Fib...
Guardado en:
Autores principales: | Massimiliano Meli, Katiuscia Pagano, Laura Ragona, Giorgio Colombo |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2014
|
Materias: | |
Acceso en línea: | https://doaj.org/article/6d46df0df8534984818e40717608e3c5 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.
por: Giorgio Colombo, et al.
Publicado: (2009) -
NMR Studies of Tau Protein in Tauopathies
por: Kristine Kitoka, et al.
Publicado: (2021) -
Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses
por: Yuki Toyama, et al.
Publicado: (2017) -
Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
por: Anders Malmendal, et al.
Publicado: (2010) -
The five-to-six-coordination transition of ferric human serum heme-albumin is allosterically-modulated by ibuprofen and warfarin: a combined XAS and MD study.
por: Carlo Meneghini, et al.
Publicado: (2014)