697 research outputs found
Rilievo tridimensionale mediante laser a scansione del cavallo ligneo del Palazzo della Ragione per il progetto di restauro
No full text
Designed 3-14-Helical β-Peptides Based on Crowned (S)-β3-H-DOPA Combined with (1S, 2S)-ACHC Residues.
No full textK. Rolka, P. Rekowski, and J. Silberring Eds., Kenes Int., Geneva, Switzerland, 2007, pp. 86-87
Linear Oligopeptides. Part 352. Synthesis, Characterization and Solution Conformational Analysis of C(alfa)-methyl-homo-phenylalanine Containing Peptides
No full textJ. CHEM. SOC. , PERKIN TRANS.
Resolving the reactor neutrino anomaly with the KATRIN neutrino experiment
No full textAbstractThe KArlsruhe TRItium Neutrino experiment (KATRIN) combines an ultra-luminous molecular tritium source with an integrating high-resolution spectrometer to gain sensitivity to the absolute mass scale of neutrinos. The projected sensitivity of the experiment on the electron neutrino mass is 200 meV at 90% C.L. With such unprecedented resolution, the experiment is also sensitive to physics beyond the Standard Model, particularly to the existence of additional sterile neutrinos at the eV mass scale. A recent analysis of available reactor data appears to favor the existence of such a sterile neutrino with a mass splitting of |Δmsterile|2⩾1.5 eV2 and mixing strength of sin22θsterile=0.17±0.08 at 95% C.L. Upcoming tritium beta decay experiments should be able to rule out or confirm the presence of the new phenomenon for a substantial fraction of the allowed parameter space
The secondary structure of a membrane-modifying peptide in a supramolecular assembly studied by PELDOR and CW-ESR spectroscopies
No full textThe 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 Angstrom which is close to the value of congruent to 14 Angstrom calculated for a 3(10)-helical structure. Estimation of the G action 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. Chern. Sec. 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
Engineering Bioinspired Luminescent Probes: Antimicrobial Peptides Chelating Lanthanide Ions.
No full textK. Rolka, P. Rekowski, and J. Silberring Eds., Kenes Int., Geneva, Switzerland, 2007, pp. 96-97
Probing the absolute mass scale of neutrinos
No full textThe Karlsruhe Tritium Neutrino (KATRIN) experiment is the next generation tritium beta decay experiment with sub-eV sensitivity to make a direct, model independent measurement of the neutrino mass. The principle of the experiment is to look for a distortion at the high energy endpoint of the electron spectrum of tritium beta decay. KATRIN will reach a final sensitivity of 200 meV at 90% C.L. on the absolute neutrino mass scale
EPR Distance Measurements in a Doubly Nitroxide-Labelled Helical β-Peptide.
No full textK. Rolka, P. Rekowski, and J. Silberring Eds., Kenes Int., Geneva, Switzerland, 2007, pp. 30-31
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