Ion transport by peptide channels has been the major theme in the work of the late P. Läuger. His theoretical and experimental approaches provided the basis for a deeper understanding of pore-mediated ion permeation through biological membranes. This review on a ligand–gated ion channel protein from the mammalian brain is dedicated to the memory of this outstanding scientist.

The scientific community will remember Peter Läuger as an exceptional man combining a generous personality and a sharp and skilful mind. He was able to attract by his views the interest of a large spectrum of biologists concerned by the mechanism of ion translocation through membranes. Yet, he was not a man with a single technique or theory. Using an authentically multidisciplinary approach, his ambition was to ‘understand transmembrane transport at the microscopic level, to capture its dynamics in the course of defined physiological processes’ (1987). According to him, ‘new concepts in the molecular physics of proteins’ had to be imagined, and ‘the traditional static picture of proteins has been replaced by the notions that proteins represent dynamic structures, subjected to conformational fluctuations covering a very wide time-range’ (1987).

The elucidation of the molecular mechanisms whereby ions and polar molecules are translocated across the hydrophobic barrier of a lipid bilayer in biological membranes is one of the most challenging problems in biological research. Specific membrane proteins, such as pumps, carriers and channels, play the central role in the various translocation pathways. Recent progress in expression cloning has provided the sequence of a number of biologically important membrane proteins and in principle the door is open to investigate every protein which might be of importance in the central signal transduction and transport processes. Unfortunately, to date there are only a few examples where the three-dimensional structure of membrane proteins are known at atomic resolution. The photosynthetic reaction centres from purple bacteria (Deisenhofer et al. 1985), bacteriorhodopsin (Henderson et al. 1990) and the large porin channel of Rhodobacter capsulata (Weiss et al. 1991). According to these structural data membrane proteins seem to fold in general in membrane-spanning α-helices and β-strands in order to saturate hydrogen bonds. Only these two motifs seem to form stable structures which can be in contact with the hydrophobic lipid interior of a membrane.

The advent of methods for forming and studying lipid bilayer membranes (Mueller et al. 1962; Hanai et al. 1964) opened the way for some fifteen years ofintensive and productive study of the properties of lipid soluble ions and ion carriers. I expect that none will dissent from the view that Peter Läuger and his associates, including R. Benz and G. Stark, did more than any other research group to advance the study of the mechanism of the charge transfer. Between 1970 and 1981 they published more than 25 substantial contributions. Thus it is appropriate that this memorial issue should contain a short review of this subject. As I have the highest regard for their work I was very pleased to be asked to write such a chapter. There is little point in providing another general survey because Läuger's group published reviews at the end of this period (Benz et al. 1980; Läuger et al. 1981) and I also reviewed the field at length (Hladky, 1979a). Instead I would like to consider the three cornerstone papers of 1971, some of the difficulties that arose from those papers, how they were overcome, and three aspects of the description that are still incomplete.

Peter Läuger introduced me (P.C.J.) to the field of ion-channel electrostatics while I was a sabbatical visitor at Konstanz in 1978–79. Läuger pointed out that the relative conductance of hydrophobic ions through phosphatidyl choline (PC) and glyceryl monooleate (GMO) membranes differed by a factor of about 100 (Hladky & Haydon, 1973), quite consistent with the difference in the water-membrane potential differences in the two systems (Pickar & Benz, 1978). However, cation conductance through gramicidin channels spanning these membranes only differs by a factor of 2–3 (Bamberg et al. 1976). Why? It is the pursuit of an answer to this question which led me into my researches in this field.