Publications by authors named "A Sadet"

Article Synopsis
  • Hyperpolarized water is being used in dynamic nuclear polarization experiments to boost NMR signals, especially for protein and peptide studies.
  • The study highlights a technique called "proton exchange-doubly relayed" nuclear Overhauser effects (NOE) to enhance signals from methyl groups in an alanine-glycine peptide.
  • By transferring hyperpolarization through a series of interactions between solvent and peptide, the researchers achieve a positive signal enhancement, which could improve NMR analysis of large proteins.
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Living systems rely on molecular building blocks with low structural symmetry. Therefore, constituent amino acids and nucleotides yield short-lived nuclear magnetic responses to electromagnetic radiation. Magnetic signals are at the basis of molecular imaging, structure determination and interaction studies.

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Imaging the molecular kinetics of antioxidants by magnetic resonance can contribute to the mechanistic understanding of therapeutic approaches. Magnetic resonance detection of the response to flashes of oxidative stress requires sequential spectroscopy on the same time scale on which reactive oxygen species are generated. To this effect, we propose a single-polarization multiple-detection stroboscopic experiment.

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Article Synopsis
  • Recent advancements in molecular symmetry-based techniques for magnetic resonance are significantly impacting areas like molecular imaging, quantum computing, and beyond.
  • The concept of effective spin symmetry, first observed in 2004, has led to the increased use of resilient spin states that allow for more detailed studies of slow processes that weren't easily accessible before.
  • Long-lived states and coherences have been developed to greatly surpass the traditional limitations of relaxation times, enabling researchers to explore new molecular behaviors and future applications in various fields.
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We introduce a new symmetry-based method for structural investigations of areas surrounding water-exchanging hydrogens in biomolecules by liquid-state nuclear magnetic resonance spectroscopy. Native structures of peptides and proteins can be solved by NMR with fair resolution, with the notable exception of labile hydrogen sites. The reason why biomolecular structures often remain elusive around exchangeable protons is that the dynamics of their exchange with the solvent hampers the observation of their signals.

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