Michael E. Green

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The genetic organization of unc-26(IV) and adjacent regions was studied in Caenorhabditis elegans. We constructed a fine structure genetic map of unc-26(IV), a gene that affects locomotion and pharyngeal muscle movement but not muscle structure. Eleven alleles were positioned relative to each other recombinationally and were classified according to(More)
Ion channels, which are found in every biological cell, regulate the concentration of electrolytes, and are responsible for multiple biological functions, including in particular the propagation of nerve impulses. The channels with the latter function are gated (opened) by a voltage signal, which allows Na(+) into the cell and K(+) out. These channels have(More)
In a previous communication (Green, 1998), the initial step in ion channel gating for voltage-gated channels was attributed to the tunneling of a proton between groups with similar p K values, under the influence of an electric field. This is in contrast to the standard thermally activated model, which leads to a "Boltzmann equation" for the gating current.(More)
A series of ab initio (density functional) calculations were carried out on side chains of a set of amino acids, plus water, from the (intracellular) gating region of the KcsA K(+) channel. Their atomic coordinates, except hydrogen, are known from X-ray structures [D.A. Doyle, J.M. Cabral, R.A. Pfuetzner, A. Kuo, J.M. Gulbis, S.L. Cohen, B.T. Chait, R.(More)
Several types of ion channels, the proteins responsible for the transport of ions across cell membranes, are described. Those of most interest are responsible for the functioning of nerve cells, and are voltage gated. Here, we propose a model for voltage gating that depends on proton transport. There are also channels that are proton-gated, of which some(More)
Phosphate ions are known to complex guanidinium groups, which are the side chains of arginine. Voltage gated channels that allow passage of ions through cell membranes, producing, for example the nerve impulse, are in many cases composed of four domains, each with six transmembrane segments. The S4 transmembrane segments of these channels have arginines(More)
Water is becoming understood as a structural element in proteins. Here we are concerned with one particular type of protein, ion channels. The S. Lividans KcsA K(+) channel, the X-ray structure of which is known, is gated by protons (i.e, by a drop in pH). Ab initio calculations suggest that an H(5)O(2) group, partially charged, connects the E118 residues(More)
A hypothesis is presented on the gating of ion channels. This is considered as a consequence, in part, of a large increase in viscosity of the water in the "vestibule" region of the channel in the high field present when the channel is not conducting. This part of gating amounts to "melting" of the high viscosity part of the water upon release of the field.(More)
Standard models of ion channel voltage gating require substantial movement of one transmembrane segment, S4, of the voltage sensing domain. Evidence comes from the accessibility to external methanethiosulfonate (MTS) reagents of the positively charged arginine residues (R) on this segment. These are first mutated to cysteines (C), which in turn react with(More)