Biomolecular electrostatics has been a subject of analysis subsequent to 3D structure determination. This situation is changing due to NMR methods we developed in the past few years [1-4]. These NMR methods allow us to quantitatively investigate biomolecular electrostatics without any use of structure information. Now, local electrostatic potentials can directly be measured for every residue of proteins and nucleic acids by these methods. The new electrostatic methods are applicable to various biomolecular processes, including protein-DNA association and liquid-liquid phase separation. Applications to intrinsically disordered proteins and conformationally flexible nucleic acids are particularly useful because structure-based analysis of electrostatics is not straightforward for such molecules. These tools also facilitate examination of theoretical models on biomolecular electrostatics.