ABSTRACT
This paper presents an analysis of the Random Telegraph Noise (RTN) of the Gate-Induced Drain Leakage (GIDL) of a Metal Oxide Semiconductor Field Effect Transistor (MOSFET). The RTN data that was measured and analytical equations are used to extract the values of the parameters for the vertical distance of the oxide trap from the interface and of the energy level of the interface trap. These values and equations allow for the distance r between the interface trap and the oxide trap to be extracted. For the first time, the accurate field enhancement factor γ(F), which depends on the magnitude of the electric field at the Si/SiO2 interface, was used to calculate the current ratio before and after the electron trapping, and the value extracted for r is completely different depending on the enhancement factor that is used.
ABSTRACT
Amyloid proteins are known to be the main cause of numerous degenerative and neurodegenerative diseases. In general, amyloids are misfolded from monomers and they tend to have ß-strand formations. These misfolded monomers are then transformed into oligomers, fibrils, and plaques. It is important to understand the forming mechanism of amyloids in order to prevent degenerative diseases to occur. Aß protein is a highly noticeable protein which causes Alzheimer's disease. It is reported that solvents affect the forming mechanism of Aß amyloids. In this research, Aß1-42 was analyzed using an all-atom MD simulation with the consideration of effects induced by two disparate solvents: water and DMSO. As a result, two different conformation changes of Aß1-42 were exhibited in each solvent. It was found that salt-bridge of Asp23 and Lys28 in Aß1-42 was the key for amyloid folding based on the various analysis including hydrogen bond, electrostatic interaction energy and salt-bridge distance. Since this salt-bridge region plays a crucial role in initiating the misfolding of Aß1-42, this research may shed a light for studies related in amyloid folding and misfolding.
