The force exerted by the membrane potential during protein import into the mitochondrial matrix

Karim Shariff*, Sandip Ghosal, Andreas Matouschek

*Corresponding author for this work

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

The force exerted on a targeting sequence by the electrical potential across the inner mitochondrial membrane is calculated on the basis of continuum electrostatics. The force is found to vary from 3.0 pN to 2.2 pN (per unit elementary charge) as the radius of the inner membrane pore (assumed aqueous) is varied from 6.5 to 12 Å, its measured range. In the present model, the decrease in force with increasing pore width arises from the shielding effect of water. Since the pore is not very much wider than the distance between water molecules, the full shielding effect of water may not be present; the extreme case of a purely membranous pore without water gives a force of 3.2 pN per unit charge, which should represent an upper limit. When applied to mitochondrial import experiments on the protein barnase, these results imply that forces between 11 ± 2 pN and 13.5 ± 2.5 pN catalyze the unfolding of barnase in those experiments. A comparison of these results with unfolding forces measured using atomic force microscopy is made.

Original languageEnglish (US)
Pages (from-to)3647-3652
Number of pages6
JournalBiophysical Journal
Volume86
Issue number6
DOIs
StatePublished - Jun 2004

ASJC Scopus subject areas

  • Biophysics

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