The use of infrared spectroscopy increases knowledge of protein structure as a complement or an alternative to other techniques. The full potential of the technique has not been developed due to some setbacks. Two-dimensional infrared spectroscopy can be of great help in extracting more information from the spectra. Two-dimensional infrared correlation maps obtained from artificial bands with known changes in band parameters give rise to characteristic patterns. Biological systems of varied complexity will give rise to 2D-IR correlation maps that reflect the changes induced by the perturbation and can be interpreted as a composite of the band simulation maps. The use in complex particles such as lipoproteins, with a lipid and a protein moiety, is a clear example of the potential of 2D-IR and how simulations help in the interpretation of the correlation maps, both in the protein and the lipid bands, distinguishing between changes only in intensity, or changes in band position or bandwidth.
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