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• W2127825477 abstract "A number of proteins can assemble into chiral structures that display strong nonlinear optical activity. For instance, proteins such as myosin and collagen exhibit intense second harmonic generation (SHG). A large number of experimental studies on the SHG of proteins have been conducted; however few predictive models have been proposed that reliably relate the macroscopic SHG properties to the amino acids present in the peptidic chain. In this study, the linear polarizability (α), first (β) and second hyperpolarizability (γ) of all twenty amino acids was investigated by time-dependent Hartree-Fock calculations under physiological conditions. Ab initio calculations were performed using the GAMESSUS computational chemistry package. We have found that the aromatic amino acids give rise to the largest mean α, β and γ values. With this finding, we hope to apply this method to protein structures in order to understand how second harmonic signal is generated from individual amino acids, as well as, recognize how manipulation of the secondary structure of proteins might enhance SHG and third harmonic generation (THG)." @default.
• W2127825477 created "2016-06-24" @default.
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• W2127825477 date "2010-11-01" @default.
• W2127825477 modified "2023-09-27" @default.
• W2127825477 title "Ab initioCalculations of the Linear and Nonlinear Optical Properties of Amino Acids" @default.
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• W2127825477 doi "https://doi.org/10.1088/1742-6596/256/1/012015" @default.
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