Using high temporal resolution single-channel electrical recordings, we have analyzed the interactions of mitochondrial presequence peptides with single TOM pores. To our knowledge, the study provides first quantitative data of the kinetics of polypeptide interaction with the mitochondrial TOM machinery reconsituted in an artificial bilayer. Romero-Ruiz, M., Mahendran, K.R., Eckert, R., Winterhalter, M., & Nussberger, S. (2010) Biophys. J., 99: 774-81
A novel mass spectrometry method termed laser-induced liquid bead ion desorption mass spectrometry (LILBID-MS) was used to determine the subunit composition and stoichiometry of the outer mitochondrial membrane protein translocon TOM. Mager, F., Sokolova, L., Lintzel, J., Brutschy, B., & Nussberger, S. (2010) Special issue: New developments in nanopore research—from fundamentals to applications, J. Physics Condensed Matter 22: 454132 (7pp)
Using high temporal resolution single-channel electrical recordings, we have analyzed the interactions of mitochondrial presequence peptides with
single TOM pores. To our knowledge, the study provides first quantitative data of the kinetics of polypeptide interaction
with the mitochondrial TOM machinery reconsituted in an artificial bilayer.
A novel mass spectrometry method termed laser-induced liquid bead ion desorption mass spectrometry (LILBID-MS)
was used to determine the subunit composition and stoichiometry of the outer mitochondrial membrane protein translocon
TOM. 
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