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We report measurements of the parity-conserving beam-normal single-spinelastic scattering asymmetries $B_n$ on $^{12}$C and $^{27}$Al, obtained withan electron beam polarized transverse to its momentum direction. Thesemeasurements add an additional kinematic point to a series of previousmeasurements of $B_n$ on $^{12}$C and provide a first measurement on $^{27}$Al.The experiment utilized the Qweak apparatus at Jefferson Lab with a beam energyof 1.158 GeV. The average lab scattering angle for both targets was 7.7degrees, and the average $Q^2$ for both targets was 0.02437 GeV$^2$ (Q=0.1561GeV). The asymmetries are $B_n$ = -10.68 $\pm$ 0.90 stat) $\pm$ 0.57 (syst) ppmfor $^{12}$C and $B_n$ = -12.16 $\pm$ 0.58 (stat) $\pm$ 0.62 (syst) ppm for$^{27}$Al. The results are consistent with theoretical predictions, and arecompared to existing data. When scaled by Z/A, the Q-dependence of all thefar-forward angle (theta < 10 degrees) data from $^{1}$H to $^{27}$Al can bedescribed by the same slope out to $Q \approx 0.35$ GeV. Larger-angle data fromother experiments in the same Q range are consistent with a slope about twiceas steep.

We report measurements of the parity-conserving beam-normal single-spinelastic scattering asymmetries $B_n$ on $^{12}$C and $^{27}$Al, obtained withan electron beam polarized transverse to its momentum direction. Thesemeasurements add an additional kinematic point to a series of previousmeasurements of $B_n$ on $^{12}$C and provide a first measurement on $^{27}$Al.The experiment utilized the Qweak apparatus at Jefferson Lab with a beam energyof 1.158 GeV. The average lab scattering angle for both targets was 7.7degrees, and the average $Q^2$ for both targets was 0.02437 GeV$^2$ (Q=0.1561GeV). The asymmetries are $B_n$ = -10.68 $\pm$ 0.90 stat) $\pm$ 0.57 (syst) ppmfor $^{12}$C and $B_n$ = -12.16 $\pm$ 0.58 (stat) $\pm$ 0.62 (syst) ppm for$^{27}$Al. The results are consistent with theoretical predictions, and arecompared to existing data. When scaled by Z/A, the Q-dependence of all thefar-forward angle (theta < 10 degrees) data from $^{1}$H to $^{27}$Al can bedescribed by the same slope out to $Q \approx 0.35$ GeV. Larger-angle data fromother experiments in the same Q range are consistent with a slope about twiceas steep.

Short-range correlations (SRCs) have been identified as being responsible for the high-momentum tail of the nucleon momentum distribution, n(k). Hard, short-range interactions of nucleon pairs generate the high-momentum tail and imprint a universal character on n(k) for all nuclei at large momentum. Triple coincidence experiments have shown a strong dominance of np pairs, but these measurements involve large final-state interactions. This paper presents the results from Jefferson Lab experiment E08014 which measured inclusive electron scattering cross section from Ca isotopes. By comparing the inclusive cross section from Ca48 to Ca40 in a kinematic region dominated by SRCs we provide a new way to study the isospin structure of SRCs.

We present new data probing short-range correlations (SRCs) in nuclei through the measurement of electron scattering off high-momentum nucleons in nuclei. The inclusive He4/He3 cross section ratio is observed to be both x and Q2 independent for 1.52, our data support the hypothesis that a previous claim of three-nucleon correlation dominance was an artifact caused by the limited resolution of the measurement. While 3N-SRCs appear to have an important contribution, our data show that isolating 3N-SRCs is significantly more complicated than for 2N-SRCs.

We address the interpretation, via an integrated computational approach, of the experimental continuous-wave electron paramagnetic resonance (cw-EPR) spectra of a complete set of conformationally highly restricted, stable 3 10 -helical peptides from hexa- to nonamers, each bis-labeled with nitroxide radical-containing TOAC (4-amino-1-oxyl-2,2,6,6-tetramethylpiperidine-4-carboxylic acid) residues. The usefulness of TOAC for this type of analysis has been shown already to be due to its cyclic piperidine side chain, which is rigidly connected to the peptide backbone α-carbon. The TOAC α-amino acids are separated by two, three, four, and five intervening residues. This set of compounds has allowed us to modulate both the radical···radical distance and the relative orientation parameters. To further validate our conclusion, a comparative analysis has been carried out on three singly TOAC-labeled peptides of similar main-chain length.

The amyloid β (A β) peptide is important in the context of Alzheimer's disease, since it is one of the major components of the fibrils that constitute amyloid plaques. Agents that can influence fibril formation are important, and of those, membrane mimics are particularly relevant, because the hydrophobic part of A β suggests a possible membrane activity of the peptide. We employed spin-label EPR to investigate the aggregation process of A β1-40 in the presence of the sodium dodecyl sulfate (SDS) detergent as a membrane-mimicking agent. In this work, the effect of SDS on A β is studied using two positions of spin label, the N-terminus and position 26. By comparing the two label positions, the effect of local mobility of the spin label is eliminated, revealing A β aggregation in the SDS concentration regime below the critical micelle concentration (CMC). We demonstrate that, at low SDS concentrations, the N-terminus of A β participates in the solubilization, most likely by being located at the particle-water interface. At higher SDS concentrations, an SDS-solubilized state that is a precursor to the one A β/micelle state above the CMC of SDS prevails. We propose that A β is membrane active and that aggregates include SDS. This study reveals the unique potential of EPR in studying A β aggregation in the presence of detergent.

The structure of the unusually long (∼100 amino-acid residues) N-terminal domain of the light-harvesting protein CP29 of plants is not defined in the crystal structure of this membrane protein. We studied the N-terminus using two electron paramagnetic resonance (EPR) approaches: the rotational diffusion of spin labels at 55 residues with continuous-wave EPR, and three sets of distances with a pulsed EPR method. The N-terminus is relatively structured. Five regions that differ considerably in their dynamics are identified. Two regions have low rotational diffusion, one of which shows α-helical character suggesting contact with the protein surface. This immobile part is flanked by two highly dynamic, unstructured regions (loops) that cover residues 10-22 and 82-91. These loops may be important for the interaction with other light-harvesting proteins. The region around residue 4 also has low rotational diffusion, presumably because it attaches noncovalently to the protein. This section is close to a phosphorylation site (Thr-6) in related proteins, such as those encoded by the Lhcb4.2 gene. Phosphorylation might influence the interaction with other antenna complexes, thereby regulating the supramolecular organization in the thylakoid membrane., (Copyright © 2014 Biophysical Society. Published by Elsevier Inc. All rights reserved.)

In this paper, we address the interpretation of molecular properties of selected singly and doubly spin-labeled peptides from continuous-wave electron spin resonance (cw-ESR) spectroscopy. This study is performed by means of an integrated computational approach that merges a stochastic treatment of long-term dynamics to ad hoc methodologies for the calculation of structural properties. In particular, our method is based on (i) the determination of geometric and local magnetic parameters of the peptides by quantum mechanical density functional calculations by taking into account solvent contribution; (ii) the hydrodynamic evaluation of dissipative properties; and (iii) molecular dynamics including equilibrium distribution of molecular conformations. The system is then described by a stochastic Liouville equation in which the spin Hamiltonian for the two electron spins, interacting with each other and coupled to two (14)N nuclear spins, is coupled to the diffusive operator describing the time evolution of slow coordinates. cw-ESR spectra are simulated for selected peptides built from the non-natural α-aminoacids α-aminoisobutyric acid (Aib) and 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC). In particular, we study the -Aib-TOAC-Aib- singly labeled tripeptide and the -Aib-TOAC-(Aib)(7)- singly labeled and -Aib-TOAC-(Aib)(5)-TOAC-Aib- doubly labeled nonapeptides. We show that good agreement is obtained with minimal resorting to fitting procedures, proving that the combination of sensitive ESR spectroscopy and sophisticated modeling is a powerful approach to the investigation of both molecular dynamics and 3D-structural properties.