With these successful demonstrations, we envision 2D-CIVS to be a powerful tool for structure determination and the study of intramolecular and intermolecular interactions through the recovery of well-resolved off-diagonal cross peaks. For example, the amide I and amide II spectral regions in peptides are highly congested and difficult to resolve at the amino acid level with condensed-phase 2D IR without the use of isotopic labeling. While traditional CIVS affords higher frequency resolution (linewidths typically 5-10 cm -1 ), experiments on small peptide systems usually require comparisons to computational predictions of many conformers and/or double resonance experiments to make structural identifications. Well-resolved cross peaks across the amide I and II regions with 2D-CIVS will help guide conformational searches and provide less ambiguity in structural assignments. Another intriguing example would be the study of biomolecule-water interactions. Solvation shell interactions are incredibly difficult to study with condensed-phase 2D IR due to the overwhelming background water signal and bulk water's rapid vibrational dynamics. Well-established clustering techniques can be used to study biomolecule-water interactions one water molecule at a time. Ultrafast pulses provide sufficient bandwidth to interrogate the amide I, amide II, and water bend transitions simultaneously. Therefore, biomolecule-water cross peaks will directly report on the water binding sites. Alternatively, if sub-ps dynamics are not critical, pulse shaping can also be used to collect spectra more rapidly in the frequency domain using few cm -1 (few ps) bandwidth pump and/or probe pulses.