Two-photon circular dichroism of molecular structures simulating L-tryptophan residues in proteins with secondary structures
Abbreviated Journal Title
Chem. Phys. Lett.
DENSITY-FUNCTIONAL THEORY; AMINO-ACIDS; ABSORPTION; SPECTROSCOPY; EXCHANGE; MODEL; IR; Chemistry, Physical; Physics, Atomic, Molecular & Chemical
Herein, we report on the calculation and the comparative analysis of the theoretical two-photon circular dichroism (TPCD) spectra of L-tryptophan (Trp) residues in proteins with secondary structures (alpha-helix, beta-strand and random coil) conformation, down to the far-UV region (FUV). The examination of the TPCD spectra of the different conformers in each configuration reveals distinctive fingerprints in the FUV, a dark spectral region for electronic circular dichroism (ECD). Our results show the potential of FUV-TPCD to identify and study protein structures in a region never assessed before but filled with important structural information. (C) 2014 Elsevier B.V. All rights reserved.
Chemical Physics Letters
"Two-photon circular dichroism of molecular structures simulating L-tryptophan residues in proteins with secondary structures" (2014). Faculty Bibliography 2010s. 6232.