Nuclear magnetic resonance (NMR) spectroscopy, and particularly solid-state NMR spectroscopy, is a method of choice to study the structure and dynamics of both the lipid and the protein components of model and biological membranes. Different approaches have been developed to study these systems in which the restricted molecular motions result in broad NMR spectra. This contribution will first p...

On the basis of in situ MAS NMR technique under flow conditions,1-4 the combined in situ MAS NMR-UV/Vis spectroscopy5 has recently been developed to obtain complimentary information on solid catalysts and, therefore, to better elucidate the mechanism involved in heterogeneous catalysis. While NMR spectroscopy allows the identification of species on the working catalyst in more detail, UV/Vis sp...

Nuclear Magnetic Resonance (NMR) spectroscopy has made a tremendous impact in many areas of chemistry, biology and medicine. In this report a student-oriented approach is presented, which enhances the ability of students to comprehend the basic concepts of NMR spectroscopy and the NMR spectra of various nuclei. The origin of chemical shifts, coupling constants, spin relaxation and the Nuclear O...

Characterisation of the structure and dynamics of large biomolecules and biomolecular complexes by NMR spectroscopy is hampered by increasing overlap and severe broadening of NMR signals. As a consequence, the number of available NMR spectroscopy data is often sparse and new approaches to provide complementary NMR spectroscopy data are needed. Paramagnetic relaxation enhancements (PREs) obtaine...