Hydrogen bonds (HBs) are among the most important noncovalent interactions in chemistry and biology. For instance, they play a key structural role in the (self-)assembly of supramolecular complexes and the folding of DNA, peptides, and proteins. Furthermore, HBs often act as essential motifs to accelerate reactions in both organocatalytic and enzymatic settings. Despite their importance, relatively few experimental methods exist that can be used to characterize HBs within a quantitative, physical framework. One such method is vibrational Stark effect (VSE) spectroscopy, which enables the measurement of local electric field strengths of specific noncovalent interactions via changes to observables in vibrational spectra. As such, VSE spectroscopy has been used to measure electric fields in solvents, at electrode interfaces, and in membranes and proteins. The VSE describes the influence of an electric field (𝐹 ⃗ ) on a vibrational frequency (𝜈̅ ; in units of cm -1 ) via the dipolar VSE equation