Olfactory perireceptor and receptor events in moths: a kinetic model revised

Modelling reveals that within about 3 ms after entering the sensillum lymph, 17% of total pheromone is enzymatically degraded while 83% is bound to the pheromone-binding protein (PBP) and thereby largely protected from enzymatic degradation. The latter proceeds within minutes, 20,000-fold more slowly than with the free pheromone. In vivo the complex pheromone–PBP interacts with the receptor molecule. At weak stimulation the half-life of the active complex is 0.8 s due to the postulated pheromone deactivation. Most likely this process is enzymatically catalysed; it changes the PBP into a scavenger form, possibly by interference with the C-terminus. The indirectly determined PBP concentration (3.8 mM) is close to direct measurements. The calculated density of receptor molecules within the plasma membrane of the receptor neuron reaches up to 6,000 units per μm2. This is compared with the estimated densities of the sensory-neuron membrane protein and of ion channels. The EC50 of the model pheromone–PBP complex interacting with the receptor molecules is 6.8 μM, as compared with the EC50 = 1.5 μM of bombykol recently determined using heterologous expression. A possible mechanism widening the range of stimulus intensities covered by the dose–response curve of the receptor-potential is proposed

The spin label amino acid TOAC and its uses in studies of peptides: chemical, physicochemical, spectroscopic, and conformational aspects

We review work on the paramagnetic amino acid 2,2,6,6-tetramethyl-N-oxyl-4-amino-4-carboxylic acid, TOAC, and its applications in studies of peptides and peptide synthesis. TOAC was the first spin label probe incorporated in peptides by means of a peptide bond. In view of the rigid character of this cyclic molecule and its attachment to the peptide backbone via a peptide bond, TOAC incorporation has been very useful to analyze backbone dynamics and peptide secondary structure. Many of these studies were performed making use of EPR spectroscopy, but other physical techniques, such as X-ray crystallography, CD, fluorescence, NMR, and FT-IR, have been employed. The use of double-labeled synthetic peptides has allowed the investigation of their secondary structure. A large number of studies have focused on the interaction of peptides, both synthetic and biologically active, with membranes. In the latter case, work has been reported on ligands and fragments of GPCR, host defense peptides, phospholamban, and β-amyloid. EPR studies of macroscopically aligned samples have provided information on the orientation of peptides in membranes. More recent studies have focused on peptide–protein and peptide–nucleic acid interactions. Moreover, TOAC has been shown to be a valuable probe for paramagnetic relaxation enhancement NMR studies of the interaction of labeled peptides with proteins. The growth of the number of TOAC-related publications suggests that this unnatural amino acid will find increasing applications in the future

A carboxyl-terminal tail peptide of neutrophil chemotactic receptor disrupts its physical complex with G protein

No abstract availabl

An analysis of lamellar x-ray diffraction from disordered membrane multilayers with application to data from retinal rod outer segments.

Oriented multilayers containing a membrane pair within the unit cell potentially possess both lattice disorder and substitution disorder. Lattice disorder occurs when there is a lack of long-range order in the lattice spacings produced by a variation in the nearest neighbor distances between unit cells. A simple form of substitution disorder can arise from a variation in the separation of the two membranes within the unit cells in the multilayer. Lattice disorder produces a monotonically increasing width for higher order lamellar "reflections" while simple substitution disorder produces an incoherent intensity underlying the coherent intensity. A generalized Patterson function analysis has been developed for treating lamellar diffraction from lattice disordered multilayers. This analysis allows the identification of the autocorrelation function of the unit cell electron density profile and its subsequent deconvolution to provide the unit cell electron density profile. A recursive procedure has been developed for separating the incoherent intensity from the coherent intensity via a Gaussian probability model of the membrane intra-pair separation. In cases studied so far both disorders can be quantitatively accounted for and eliminated from interfering with the phasing of the coherent intensity or distorting the derived electron density profile. Lamellar X-ray diffraction data from intact retinal rods, using either film or position sensitive detectors, shows severe effects of both forms of disorder which have not been taken into account in past analysis of such data. We have applied our analysis to the data on dark adapted rod outer segments in electrophysiologically intact retinas of Chabre and Cavaggioni (unpublished). An electron density profile is derived at 25 A resolution. The lattice nearest neighbor spacing has a variation of +/- 19 A out of a 295 A repeat. The intra-unit cell membrane pair center to center distance of 88 A varies +/-8 A