The frequency distributions in Figure show that LE7b has a significantly blue-shifted distribution of water compared to LK7b, suggesting weaker hydrogen bonds of water surrounding the protein. This is consistent with past findings of molecular dynamics studies that LE7b is less stable than LK7b in terms of backbone hydrogen bonds. Our prior experiments show that the main N-H peak is blue-shifted in LE7b (Figure ). This dominant N-H contribution masks the O-H peaks, and thus the O-H stretch frequencies remained elusive in the analysis using the conventional fitting method (Figure ). The new fitting clearly shows that the water signal is also blue-shifted in the experimental spectra, unveiling the agreement with previously reported computational O-H stretch spectra. These blue shifts of water O-H stretches and protein N-H stretches reveal that LE7b has a relatively lower ability to form a coherent water supramolecular structure and is less stable intrinsically. Although our previous molecular dynamics studies already demonstrated the correlation between water O-H stretches and protein N-H stretches, the new fitting model allows us to reliably extract the O-H stretching frequencies of water in the first hydration shell from experiments, thereby validating the correlation. This combined experimental and computational result has a profound implication -the stability of a protein and its hydration shell can be intimately connected.