Since the early days of NMR, spectroscopists are fighting a permanent battle for more sensitivity and higher spectral resolution. In this presentation, I will address some of the developments I had the chance to contribute to. Isotopic labeling has been a crucial step for the structural investigation of proteins by NMR, allowing the recording of high-dimensional correlation spectra between various heteronuclei (¹H, ¹³C, ¹⁵N, …). In the case of nanocrystalline proteins, however, uniform carbon-13 labeling limits spectral resolution due to the presence of ¹³C-¹³C scalar couplings. In a first example, I will show how spin-state selective correlation techniques in solid-state NMR of proteins can be used to overcome some of these problems, thus providing a substantial gain in spectral resolution. A second application concerns the bacterial cell wall, a giant non-crystalline biopolymer. Despite its huge size, high-resolution solid-state NMR spectra can be obtained because of the high degree of internal dynamics present in this heterogeneous biomolecular system. Information on structural features or interaction sites is obtained as site-resolved modifications of the polymer mobility.  Addressing biomolecular systems of increasing size becomes a challenge in terms of experimental sensitivity. In the last part of my presentation, I will introduce Dynamic Nuclear Polarization  (DNP), a hyperpolarization technique that allows boosting the sensitivity of solid-state NMR spectroscopy. I will focus on the selective DNP (sel-DNP) approach we recently introduced for the study of biomolecular interaction sites. When most biomolecular systems present a strongly degraded spectral resolution under DNP conditions, Sel-DNP  provides highly resolved spectra for the binding region of interest.

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