Dynamics of heme complexed with human serum albumin: a theoretical approach.
Eur Biophys J
; 41(12): 1033-42, 2012 Dec.
Article
em En
| MEDLINE
| ID: mdl-23104623
Human serum albumin (HSA) is the most abundant protein in the blood serum. It binds several ligands and has an especially strong affinity for heme, hence becoming a natural candidate for oxygen transport. In order to analyze the interaction of HSA-heme, molecular dynamics simulations of HSA with bound heme were performed. Based on the results of X-ray diffraction, the binding site of the heme, localized in subdomain IB, was considered. We analyzed the fluctuations and their correlations along trajectories to detect collective motions. The role of H bonds and salt bridges in the stabilization of heme in its pocket was also investigated. Complementarily, the localization of water molecules in the hydrophobic pocket and the interaction with heme were discussed.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Albumina Sérica
/
Simulação de Dinâmica Molecular
/
Heme
Limite:
Humans
Idioma:
En
Revista:
Eur Biophys J
Assunto da revista:
BIOFISICA
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Alemanha