Modelling and analysis of an open-loop induction motor drive incorporating the effect of inverter dead-time

The objective of this paper is to study the influence of inverter dead-time on steady as well as dynamic operation of an open-loop induction motor drive fed from a voltage source inverter (VSI). Towards this goal, this paper presents a systematic derivation of a dynamic model for an inverter-fed induction motor, incorporating the effect of inverter dead-time, in the synchronously revolving dq reference frame. Simulation results based on this dynamic model bring out the impact of inverter dead-time on both the transient response and steady-state operation of the motor drive. For the purpose of steady-state analysis, the dynamic model of the motor drive is used to derive a steady-state model, which is found to be non-linear. The steady-state model shows that the impact of dead-time can be seen as an additional resistance in the stator circuit, whose value depends on the stator current. Towards precise evaluation of this dead-time equivalent resistance, an analytical expression is proposed for the same in terms of inverter dead-time, switching frequency, modulation index and load impedance. The notion of dead-time equivalent resistance is shown to simplify the solution of the non-linear steady-state model. The analytically evaluated steady-state solutions are validated through numerical simulations and experiments.

Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue96 in the Plasmodial Enzyme

Despite extensive research into triosephosphate isomerases (TIMs), there exists a gap in understanding of the remarkable conjunction between catalytic loop-6 (residues 166-176) movement and the conformational flip of Glu165 (catalytic base) upon substrate binding that primes the active site for efficient catalysis. The overwhelming occurrence of serine at position96 (98% of the 6277 unique TIM sequences), spatially proximal to E165 and the loop-6 residues, raises questions about its role in catalysis. Notably, Plasmodium falciparum TIM has an extremely rare residuephenylalanineat this position whereas, curiously, the mutant F96S was catalytically defective. We have obtained insights into the influence of residue96 on the loop-6 conformational flip and E165 positioning by combining kinetic and structural studies on the PfTIM F96 mutants F96Y, F96A, F96S/S73A, and F96S/L167V with sequence conservation analysis and comparative analysis of the available apo and holo structures of the enzyme from diverse organisms.