Slip dynamics at a patterned rubber/glass interface during stick-slip motions.

We report on an experimental study of heterogeneous slip instabilities generated during stick-slip motions at a contact interface between a smooth rubber substrate and a patterned glass lens. Using a sol-gel process, the glass lens is patterned with a lattice of parallel ridges (wavelength, 1.6 μm, amplitude 0.

Structural determinants for high-affinity zolpidem binding to GABA-A receptors.

The imidazopyridine zolpidem (Ambien) is one of the most commonly prescribed sleep aids in the United States (Rush, 1998). Similar to classic benzodiazepines (BZDs), zolpidem binds at the extracellular N-terminal alpha/gamma subunit interface of the GABA-A receptor (GABAR). However, zolpidem differs significantly from classic BZDs in chemical structure and neuropharmacological properties.

Structural requirements for imidazobenzodiazepine binding to GABA(A) receptors.

Several structural subclasses of ligands bind to the benzodiazepine (BZD) binding site of the GABA(A) receptor. Previous studies from this laboratory have suggested that imidazobenzodiazepines (i-BZDs, e.g.

A (beta)-strand in the (gamma)2 subunit lines the benzodiazepine binding site of the GABA A receptor: structural rearrangements detected during channel gating.

Benzodiazepines (BZDs) exert their effects in the CNS by binding to a modulatory site on GABA(A) receptors. Individual amino acids have been implicated in BZD recognition and modulation of the GABA(A) receptor, but the secondary structure of the amino acids contributing to the BZD binding site has not been elucidated. In this report we used the substituted cysteine accessibility method to understand the structural dynamics of a region of the GABA(A) receptor implicated in BZD binding, gamma(2)Y72-gamma(2)Y83.