Carregant...
Carregant...

Vés al contingut (premeu Retorn)

Computational study of the free energy landscape of the miniprotein CLN025 in explicit and implicit solvent

Autor
Rodríguez, A.; Mokoema, P.; Corcho, F.; Bisetty, K.; Perez, J.
Tipus d'activitat
Article en revista
Revista
Journal of physical chemistry B
Data de publicació
2010-02-17
Volum
115
Número
6
Pàgina inicial
1440
Pàgina final
1449
DOI
https://doi.org/10.1021/jp106475c Obrir en finestra nova
Repositori
http://hdl.handle.net/2117/12061 Obrir en finestra nova
Resum
The prediction capabilities of atomistic simulations of peptides are hampered by different difficulties, including the reliability of force fields, the treatment of the solvent or the adequate sampling of the conformational space. In this work, we have studied the conformational profile of the 10 residue miniprotein CLN025 known to exhibit a β-hairpin in its native state to understand the limitations of implicit methods to describe solvent effects and how these may be compensated by using diffe...
Citació
Rodríguez, A. [et al.]. Computational study of the free energy landscape of the miniprotein CLN025 in explicit and implicit solvent. "Journal of physical chemistry B", 17 Febrer 2010, vol. 115, núm. 6, p. 1440-1449.
Grup de recerca
CEBIM - Centre de Biotecnologia Molecular
ENGMOL - Enginyeria Molecular

Participants