Abstract
A tutorial is provided for the generalized two-dimensional correlation spectroscopy (2DCOS), which is applicable to the vibrational spectroscopic study of proteins and related systems. In 2DCOS, similarity or dissimilarity among variations of spectroscopic intensities, which are induced by applying an external perturbation to the sample, is examined by constructing correlation spectra defined by two independent spectral variable axes. By spreading congested or overlapped peaks along the second dimension, apparent spectral resolution is enhanced and interpretation of complex spectra becomes simplified. A set of simple rules for the intensities and signs of correlation peaks is used to extract insightful information. Simulated IR spectra for a model protein are used to demonstrate the specific utility of 2DCOS. Additional tools useful in the 2DCOS analysis of proteins, such as data segmentation assisted with moving-window analysis, 2D codistribution analysis, Pareto scaling, and null-space projection are also discussed.
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