Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility
The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for difference...
Guardado en:
Autores principales: | Fernandez-Alberti, S., Bacelo, D. E., Binning Jr., R. C., Echave, Julián, Chergui, M., Lopez-Garriga, J. |
---|---|
Formato: | Articulo |
Lenguaje: | Inglés |
Publicado: |
2006
|
Materias: | |
Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/83269 |
Aporte de: |
Ejemplares similares
-
Sulfide binding properties of truncated hemoglobins
Publicado: (2010) -
Sulfide binding properties of truncated hemoglobins
por: Nicoletti, F.P., et al. -
The role of hydration on the mechanism of allosteric regulation: In situ measurements of the oxygen-linked kinetics of water binding to hemoglobin
por: Salvay, Andrés Gerardo, et al.
Publicado: (2003) -
Ligand uptake in Mycobacterium tuberculosis truncated hemoglobins is controlled by both internal tunnels and active site water molecules
por: Boechi, Leonardo, et al.
Publicado: (2015) -
Ligand uptake in Mycobacterium tuberculosis truncated hemoglobins is controlled by both internal tunnels and active site water molecules
por: Boechi, L., et al.