Abstract
Quantitative measurements of protein orientation and secondary structure composition are of great importance for protein biotechnology applications and disease treatments, and yet, they are technically challenging for a spectroscopic study. On the basis of quantum mechanics/molecular mechanics simulations, we demonstrate that two-dimensional (2D) linear dichroism spectroscopy is capable of probing the direction of α-helix motifs in proteins. Compared to the conventional linear dichroism (LD) spectra, 2D spectra double the measurable range of orientation of secondary structures. In addition, by calculating the ratio of transverse ππ* signals to longitudinal ππ* signals in 2D spectra, we can achieve quantitative measurement of the fraction of α-helix content in a protein.
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