Ligand Discrimination in Myoglobin from Linear-Scaling DFT+U.
J Phys Chem Lett
; 3(11): 1448-52, 2012 Jun 07.
Article
en En
| MEDLINE
| ID: mdl-26285620
ABSTRACT
Myoglobin modulates the binding of diatomic molecules to its heme group via hydrogen-bonding and steric interactions with neighboring residues, and is an important benchmark for computational studies of biomolecules. We have performed calculations on the heme binding site and a significant proportion of the protein environment (more than 1000 atoms) using linear-scaling density functional theory and the DFT+U method to correct for self-interaction errors associated with localized 3d states. We confirm both the hydrogen-bonding nature of the discrimination effect (3.6 kcal/mol) and assumptions that the relative strain energy stored in the protein is low (less than 1 kcal/mol). Our calculations significantly widen the scope for tackling problems in drug design and enzymology, especially in cases where electron localization, allostery, or long-ranged polarization influence ligand binding and reaction.
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1
Banco de datos:
MEDLINE
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
J Phys Chem Lett
Año:
2012
Tipo del documento:
Article
País de afiliación:
Reino Unido