Breakdown of the Debye polarization ansatz at protein-water interfaces

ARIEL FERNANDEZ

JOURNAL OF CHEMICAL PHYSICS

AMER INST PHYSICS

Lugar: New York; Año: 2013 vol. 138 p. 225103 - 225103

0021-9606

The topographical and physico-chemical complexity of protein-water interfaces scales down to the sub-nanoscale range. At this level of confinement, we demonstrate that the dielectric structure of interfacial water entails a breakdown of the Debye ansatz that postulates the alignment of polarization with the protein electrostatic field. The tendencies to promote anomalous polarization are determined for each residue type and a particular kind of structural defect is shown to provide the predominant causal context. © 2013 AIP Publishing LLC. [http://dx.doi.org/10.1063/1.4810867] with the protein electrostatic field. The tendencies to promote anomalous polarization are determined for each residue type and a particular kind of structural defect is shown to provide the predominant causal context. © 2013 AIP Publishing LLC. [http://dx.doi.org/10.1063/1.4810867] with the protein electrostatic field. The tendencies to promote anomalous polarization are determined for each residue type and a particular kind of structural defect is shown to provide the predominant causal context. © 2013 AIP Publishing LLC. [http://dx.doi.org/10.1063/1.4810867] ansatz that postulates the alignment of polarization with the protein electrostatic field. The tendencies to promote anomalous polarization are determined for each residue type and a particular kind of structural defect is shown to provide the predominant causal context. © 2013 AIP Publishing LLC. [http://dx.doi.org/10.1063/1.4810867]© 2013 AIP Publishing LLC. [http://dx.doi.org/10.1063/1.4810867]