The papers related to the theoretical background and experimental investigations by pulsed electron double resonance (PELDOR) are reviewed. The main aim of this pulsed ESR application is to study the dipole-dipole spin interaction. In PELDOR the ESR spectrum is excited by two ESE pulses at frequency w, and additional pumping pulse at tob. Decay function V(T) of the ESE signal, when the time interval T between the first ESE pulse and pumping pulse is varied, contains the information on dipole-dipole couplings in the spin system. The kinetics of V(T) decay strongly depends upon distance, mutual orientation inside interacting spin pairs and space distribution of radicals throughout the sample. The distances between spins which were measured or estimated using PELDOR in the papers reviewed are in the range of 15= 130 A. This pulsed ESR technique turns now to be a powerful supplement to conventional ESE in studying the free radicals space distribution..

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A new technique is described that is suitable to determine the formation of aggregates from monomeric biomolecules. This technique has been tested in the study of the self-assembling properties of the antibiotic trichogin GA IV which belongs to the class of peptaibols. We have investigated the self-assembling properties of three trichogin analogues by pulsed double resonance in electron spin−echo (PELDOR) spectroscopy combined with conventional continuous wave ESR spectroscopy. In the peptides examined Aib has been substituted by its spin-labeled analogue TOAC at three specific positions of the sequence. More specifically, the magnetic dipole−dipole relaxation of the spin-labeled peptides is measured in glassy polar and apolar solvents at 77 K. Specific assemblies of trichogin molecules are formed in an apolar solvent but addition of a more polar solvent leads to dissociation of the aggregates. The estimates based on experimental data show that each aggregate cluster contains four peptide molecules. Some of the distances between spin labels in the cluster have been determined. In addition, CW-ESR data suggest the occurrence of aggregated species in the same solutions at room temperature. The experimental results are consistent with a model wherein four amphiphilic helical peptide molecules form a vesicular system with the polar amino acid side chains pointing to the interior and the apolar side chains to the exterior of the cluster.

We show how it is possible to use the plethystic program in order to compute baryonic generating functions that count BPS operators in the chiral ring of quiver gauge theories living on the world volume of D branes probing a non compact CY manifold. Special attention is given to the conifold theory and the orbifold C 2 Z 2 × C, where exact expressions for generating functions are given in detail. This paper solves a long standing problem for the combinatorics of quiver gauge theories with baryonic moduli spaces. It opens the way to a statistical analysis of quiver theories on baryonic branches. Surprisingly, the baryonic charge turns out to be the quantized Kähler modulus of the geometry.

The new technique of pulsed electron-electron double resonance in electron spin-echo (PELDOR) in combination with the CW-ESR method has been used to investigate the secondary structure of a double spin-labeled peptide (the [TOAC-1,8]-analogue of the peptaibol antibiotic trichogin GA IV) that is hidden into a tetrameric supramolecular assembly of unlabeled peptide molecules. The magnetic dipole-dipole relaxation of spin labels has been experimentally studied in glassy solutions of the double-labeled peptide frozen to 77 K in a mixture of chloroform-toluene with an excess of unlabeled peptide. The PELDOR signal oscillations have been observed at high degrees of dilution with unlabeled peptide. The intramolecular distance between the spin labels of the peptide molecule in the aggregate has been determined from the oscillation frequency to be 15.7 A which is close to the value of (approximately equal to) 14 A calculated for a 3(10)-helical structure. Estimation of the fraction of this ordered secondary structure shows that about 19% of the peptide molecules in aggregates are folded in the 3(10)-helical conformation. The present experimental results are consistent with our molecular model presented in J. Am. Chem. Soc. 2000, 122, 3843-3848, wherein four amphiphilic 3(10)-helical peptide molecules form a vesicular system with the polar amino acid side chains pointing to the interior, and the apolar side chains, to the exterior of the cluster. The experimental data were compared with the results obtained with other techniques.

The lipopeptaibol trichogin GA IV is a 10 amino acid-long residue and alpha-aminoisobutyric acid-rich antibiotic peptide of fungal origin. TOAC (2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid) spin-labeled analogs of this membrane active peptide were investigated in hydrated bilayers of dipalmitoylphosphatidylcholine by electron spin echo envelope modulation (ESEEM) spectroscopy and pulsed electron-electron double resonance (PELDOR). Since, the ESEEM of the spin label appears to be strongly dependent on the presence of water molecules penetrated into the membrane, this phenomenon was used to study the location of this peptide in the membrane. This was achieved by comparing the ESEEM spectra for peptides labeled at different positions along the amino acid sequence with spectra known for lipids with spin labels at different positions along the hydrocarbon chain. To increase the ESEEM amplitude and to distinguish the hydrogen nuclei of water from lipid protons, membranes were hydrated with deuterated water. The PELDOR spectroscopy technique was chosen to study peptide aggregation and to determine the mutual distance distribution of the spin-labeled peptides in the membrane. The location of the peptide in the membrane and its aggregation state were found to be dependent on the peptide concentration. At a low peptide/lipid molar ratio (less than 1:100) the nonaggregated peptide chain of the trichogin molecules lie parallel to the membrane surface, with TOAC at the 4th residue located near the 9th-11th carbon positions of the sn-2 lipid chain. Increasing this ratio up to 1:20 leads to a change in peptide orientation, with the N-terminus of the peptide buried deeper into membrane. Under these conditions peptide aggregates are formed with a mean aggregate number of about N = 2. The aggregates are further characterized by a broad range of intermolecular distances (1.5-4 nm) between the labels at the N-terminal residues. The major population exhibits a distance of approximately 2.5 nm, which is of the same order as the length of the helical peptide. We suggest that the constituting monomers of the dimer are antiparallel oriented.

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Abstraet. Double electron-electron resonance in electron spin echo has been used to study the glassy solutions of poly-4-vinylpyridine doped by nitroxyl radieals frozen in liquid nitrogen. The phase relaxation of spin labels due to spin-spin interaction of unpaired electrons has been studied. The intramolecular and intermolecular contributions of the dipole-dipole interaction of spin labels into relaxation process have been separated. Ir has been established that both the intramolecular and intermolecular spin-spin interaction of spin labels lead to the dependence of echo signal on time T of the exp(-aŸ type. It is shown that for ~e intramoleeular interaction the experimental q value is 0.3, for the intermolecular one it is 2. The assumption has been made of the linear structure of polyme¡ molecules due to the presente of a sufficiently high density of ah electric charge on polymeric molecules.