We evaluated the strenghts of the method (in terms of resolution and sensitivity) on a number of proteins, ranging from small model ones (GB1, MNEI) to complex and dynamic protein assemblies: fibrils (HET-s), viral capsids (AP205, HIV-1) or oligomers from E. coli replisome (DnaB), under >100 kHz magic-angle spinning and at the highest magnetic field commercially available. Despite a certain loss in resolution of 1H resonances, we lean towards the full protonation of proteins as a simpler and more general method of sample preparation for solid-state NMR compared to approaches based on extensive deuteration. We demonstrated that large protonated proteins such as those from E. coli replisome can be immobilised by sedimentation, and studied with ssNMR without a significant penalty in resolution. We developed new sensitive methods for the efficient resonance assignment in proteins and ribonucleic acids, which are applicable thanks to improved spectral properties at ultrafast MAS conditions. We also proposed methods to report on proton-proton proximities that allow a determination of three-dimensional structures of fully protonated proteins. New labelling schemes were devised to assist structure modelling of assemblies. These methodological advances were communicated to broad audience of general chemistry and biology journals, and are already exploited in NMR groups world-wide.