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

被引：4
|
作者：
Vesga, Yuly [1 ]
Diaz, Carlos [1 ]
Hernandez, Florencio E. [1 ,2 ]
机构：
[1] Univ Cent Florida, Dept Chem, Orlando, FL 32816 USA
[2] Univ Cent Florida, CREOL, Coll Opt & Photon, Orlando, FL 32816 USA
来源：
RSC ADVANCES | 2014年 / 4卷 / 105期
基金：
美国国家科学基金会;
关键词：
DENSITY-FUNCTIONAL THEORY; ABSORPTION; SPECTROSCOPY; MODEL; IR;
D O I：
10.1039/c4ra08383k
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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 (alpha-helix, beta-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.
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页码：60974 / 60986
页数：13
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