Vibrational Spectroscopy of Molecular Interactions

Vibrational spectroscopy encompasses a suite of techniques that probe the characteristic vibrational motions of molecules, revealing intimate details of bond strengths, structural motifs and intermolecular forces. In the infrared region, absorption or scattering processes induce transitions between quantised vibrational states, producing signature bands that serve as fingerprints of chemical environments. Raman spectroscopy complements infrared methods by detecting inelastically scattered light, often providing access to vibrations that are weak or forbidden in the IR spectrum. Over the past decade, the advent of ultrafast laser sources and multidimensional approaches has transformed vibrational spectroscopy into a powerful tool for studying dynamic processes in real time. Two-dimensional infrared (2D-IR) spectroscopy, for example, correlates excitation and detection frequencies to elucidate coupling between vibrational modes, spectral diffusion and energy-transfer pathways on femtosecond to picosecond timescales. When applied to complex systems such as proteins, electrolytes or solid-state materials, these methods reveal how hydrogen bonding, solvation shells and local electric fields govern function and reactivity. Recent technical innovations—including high-repetition-rate mid-IR pulse shaping, phase cycling and microscopy configurations—have extended spatial and temporal resolution, enabling researchers to image heterogeneity in living cells, monitor ion transport in battery electrolytes and screen biomolecular interactions in high throughput. The global significance of these advances spans from fundamental studies of protein folding and enzyme catalysis to the development of next-generation energy materials and diagnostic assays.

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Vibrational Spectroscopy of Molecular Interactions publication trend

The graph below shows the total number of articles in vibrational spectroscopy of molecular interactions across all publications each year (not limited to Nature Index journals).

Technical terms

Vibrational spectroscopy: A set of analytical techniques that measure the energy absorbed or scattered when molecular vibrations are excited, yielding information on bond strengths and chemical environments.

Two-dimensional infrared (2D-IR) spectroscopy: An advanced technique correlating excitation and detection frequencies to map couplings and dynamic processes among vibrational modes on ultrafast timescales.

Amide I band: A prominent infrared absorption feature around 1,650 cm⁻¹ arising predominantly from the C=O stretching vibration in peptide backbones, widely used to probe protein secondary structure.

Spectral diffusion: The time-dependent fluctuation of vibrational frequencies due to changes in local environment, revealing solvent dynamics and molecular reorganisation.

Solvatochromism: The shift in vibrational or electronic absorption frequencies of a probe molecule caused by interactions with surrounding solvent molecules.

References

1. Using 2D-IR Spectroscopy to Measure the Structure, Dynamics, and Intermolecular Interactions of Proteins in H2O. Accounts of Chemical Research (2024).
2. Biomolecular infrared spectroscopy: making time for dynamics. Chemical Science (2024).
3. 2D IR spectroscopy at 100 kHz utilizing a Mid-IR OPCPA laser source.. Optics Express (2016).
4. Enhancing signal detection and completely eliminating scattering using quasi-phase-cycling in 2D IR experiments.. Optics Express (2010).
5. Ultrafast 2D IR microscopy. Optics Express (2014).
6. Rapid Screening of DNA–Ligand Complexes via 2D-IR Spectroscopy and ANOVA–PCA. Analytical Chemistry (2018).
7. Characterization of Acetonitrile Isotopologues as Vibrational Probes of Electrolytes. The Journal of Physical Chemistry B (2021).