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Issue 105, 2014
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Theoretical study of two-photon circular dichroism on molecular structures simulating aromatic amino acid residues in proteins with secondary structures

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Abstract

Herein, we report on the calculation and the comparative analysis of the theoretical two-photon circular dichroism (TPCD) spectra of L-histidine (His), L-phenylalanine (Phe), and L-tyrosine (Tyr) simulating residues in proteins with secondary structures (α-helix, β-strand and random coil), down to the far-UV region (FUV). This work exposes unique signatures in the FUV for each conformer in each configuration. The outcomes of this research show how FUV-TPCD can be used to study peptide and protein structures in a region never evaluated before but packed with important structural information.

Graphical abstract: Theoretical study of two-photon circular dichroism on molecular structures simulating aromatic amino acid residues in proteins with secondary structures

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Article information


Submitted
08 Aug 2014
Accepted
10 Nov 2014
First published
10 Nov 2014

RSC Adv., 2014,4, 60974-60986
Article type
Paper
Author version available

Theoretical study of two-photon circular dichroism on molecular structures simulating aromatic amino acid residues in proteins with secondary structures

Y. Vesga, C. Diaz and F. E. Hernandez, RSC Adv., 2014, 4, 60974
DOI: 10.1039/C4RA08383K

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