Publications by authors named "A Vanas"

To characterize structure and molecular order in the nanometre range, distances between electron spins and their distributions can be measured via dipolar spin-spin interactions by different pulsed electron paramagnetic resonance experiments. Here, for the single-frequency technique for refocusing dipolar couplings (SIFTER), the buildup of dipolar modulation signal and intermolecular contributions is analysed for a uniform random distribution of monoradicals and biradicals in frozen glassy solvent by using the product operator formalism for electron spin . A dipolar oscillation artefact appearing at both ends of the SIFTER time trace is predicted, which originates from the weak coherence transfer between biradicals.

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Protein aggregation into amyloid fibrils is associated with multiple neurodegenerative diseases, including Parkinson's disease. Kinetic data and biophysical characterization have shown that the secondary nucleation pathway highly accelerates aggregation via the absorption of monomeric protein on the surface of amyloid fibrils. Here, we used NMR and electron paramagnetic resonance spectroscopy to investigate the interaction of monomeric α-synuclein (α-Syn) with its fibrillar form.

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Distance measurement in the nanometre range is among the most important applications of pulse electron paramagnetic resonance today, especially in biological applications. The longest distance that can be measured by all presently used pulse sequences is determined by the phase memory time of the observed spins. Here we show that one can measure the dipolar coupling strong microwave irradiation by using an appropriate frequency- or phase-modulation scheme, i.

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Finland trityl radical (FTR) shows very attractive EPR spectroscopic properties for a manifold of applications. For most of its applications only one chemically reactive functional group is needed. The presence of three equally reactive carboxyl groups leads to FTR modifications through reactions which give statistical mixtures of 1-fold-, 2-fold-, and 3-fold-modified and unmodified FTR.

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Article Synopsis
  • A new statistical method is introduced for analyzing paramagnetic relaxation enhancement (PRE) and paramagnetic relaxation interference (PRI) data using correlation matrices in nuclear magnetic resonance (NMR) studies.
  • The technique is illustrated with the proteins osteopontin (OPN) and brain acid soluble protein 1 (BASP1), both of which are intrinsically disordered proteins (IDPs).
  • This correlation analysis reveals detailed insights into how IDPs undergo conformational averaging and demonstrates the correlated structural fluctuations within their individual sub-domains.
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