Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study

NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exact...

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Detalles Bibliográficos
Autores principales: Petruk, A.A., Vergara, A., Estrin, D., Merlino, A.
Formato: JOUR
Materias:
Molecular dynamics
Nitric oxide
Nitrosylhemoglobin
heme
hemoglobin
hemoglobin alpha chain
hemoglobin beta chain
nitric oxide
article
controlled study
density functional theory
hydration
ligand binding
molecular dynamics
nitrosylation
priority journal
protein conformation
protein tertiary structure
Hemoglobins
Humans
Molecular Dynamics Simulation
Nitric Oxide
Protein Structure, Quaternary
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00145793_v587_n15_p2393_Petruk
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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