Corrigendum to "The impact of phonon-assisted tunneling on optical and quantum characteristics of a coupled two-quantum dot system" [Heliyon 9 (8), August 2023 Article e18451].

[This corrects the article DOI: 10.1016/j.heliyon.2023.e18451.].

The impact of phonon-assisted tunneling on optical and quantum characteristics of a coupled two-quantum dot system.

This work investigates the impact of decoherence induced by pure dephasing and phonon-assisted tunneling mechanisms on the optical and quantum properties of two quantum dots. Special attention is given to the density matrix at steady state, and a detailed analysis of populations, coherences, optical transitions and the emission spectrum is performed. Additionally, we study the influence of both phonon-decoherence mechanisms on bipartite entanglement and the degree of mixedness of the system. In particular, our findings indicate that the phonon-assisted tunneling mechanism partially affects the coherences of the system and quantum properties when the imbalance of phonon absorption and emission is significant. Conversely, the pure dephasing mechanism does not affect the populations but strongly entangles the quantum dots and the reservoir, inducing maximally mixed states and significantly reducing the spectral splitting in the emission spectrum of the system.

Terahertz Frequency Spectroscopy to Determine Cold Shock Protein Stability upon Solvation and Evaporation - A Molecular Dynamics Study.

Infrared (IR) and Terahertz (THz) spectroscopy simulations were carried out using CHARMM35b2 to determine protein stability. The stabilities of three bacterial cold shock proteins (Csps) originating from mesophiles, thermophiles and hyper- thermophiles respectively were investigated in this study. The three different Csps were investigated by Normal-Mode analysis and Molecular Dynamics simulation of THz spectra using the Hessian matrix for solvated systems, interpreted in the harmonic approximation at optimum near-melting temperatures of each homologue, by incorporating differences in the hydrous and anhydrous states of the Csps. The results show slight variations in the large scale protein motion. However, the IR spectra of Csps observed at the low frequency saddle surface region, clearly distinguishes the thermophilic and mesophilic proteins based on their stability. Further studies on protein stability employing low-frequency collective modes have the potential to reveal functionally important conformational changes that are biologically significant.