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Biophys J. 1997 Dec;73(6):2980-9.

Influence of the membrane potential on the free energy of an intrinsic protein.

Author information

1
Département de physique, Université de Montréal, Québec, Canada. rouxb@plgcn.umontreal.ca

Abstract

A modified Poisson-Boltzmann equation is developed from statistical mechanical considerations to describe the influence of the transmembrane potential on macromolecular systems. Using a Green's function formalism, the electrostatic free energy of a protein associated with the membrane is expressed as the sum of three terms: a contribution from the energy required to charge the system's capacitance, a contribution corresponding to the interaction of the protein charges with the membrane potential, and a contribution corresponding to a voltage-independent reaction field free energy. The membrane potential, which is due to the polarization interface, is calculated in the absence of the protein charges, whereas the reaction field is calculated in the absence of transmembrane potential. Variations in the capacitive energy associated with typical molecular processes are negligible under physiological conditions. The formulation of the theory is closely related to standard algorithms used to solve the Poisson-Boltzmann equation and only small modifications to current source codes are required for its implementation. The theory is illustrated by examining the voltage-dependent membrane insertion of a simple polyalanine alpha-helix and by computing the electrostatic potential across a 60-A-diameter sphere meant to represent a large intrinsic protein.

PMID:
9414213
PMCID:
PMC1181204
DOI:
10.1016/S0006-3495(97)78327-9
[Indexed for MEDLINE]
Free PMC Article

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