Microgrid Disaster Resiliency Analysis: Reducing Costs in Continuity of Operations (COOP) Planning

The electric grid serves a vital role in the supply chain of nearly all industrial and commercial organizations. A Microgrid infrastructure can provide this service and beneficial non-emergency services including a variety of generation/energy sources. To demonstrate the applicability of microgrids for energy resiliency, we present a microgrid resiliency case study for United Parcel Service’s (UPS) three separate shipping facilities. The goal, to enhance energy security, minimize cost and prevent cascading losses within other related business units. The impacts and consequences of which are quantified in this study using a Mean Failure Cost (MFC) risk assessment measure. MFC accounts for the potential loses to identified stakeholders that may result from a set of identified failures due to a set of identified threats. In this case, our study uses a method we call All Hazards Econometric System (AHES). AHES incorporates the cost of COOP using a strategy that considers the payback period of microgrid installation as compared to other energy delivery strategies

Fast Quasi-Static Time-Series Simulation for Accurate PV Inverter Semiconductor Fatigue Analysis with a Long-Term Solar Profile

Power system simulations with long-term data typically have large time steps, varying from one second to a few minutes. However, for PV inverter semiconductors in grid-connected applications, the minimum thermal stress cycle occurs over the fundamental grid frequency (50 or 60 Hz). This requires the time step of the fatigue simulation to be approximately 100 μs. This small time step requires long computation times to process yearly power production profiles. In this paper, we propose a fast fatigue simulation for inverter semiconductors using the quasi-static time-series simulation concept. The proposed simulation calculates the steady state of the semiconductor junction temperature using a fast Fourier transform. The small thermal cycling during a switching period and even over the fundamental waveform is disregarded to further accelerate the simulation speed. The resulting time step of the fatigue simulation is 15 min, which is consistent with the solar dataset. The error of the proposed simulation is 0.16% compared to the fatigue simulation results using the complete thermal stress profile. The error of the proposed method is significantly less than the conventional averaged thermal profile. A PV inverter that responds to a transactive energy system is simulated to demonstrate the use of the proposed fatigue simulation. The proposed simulation has the potential to cosimulate with system-level simulation tools that also adopt the quasi-static time-series concept

The 1.6-Å crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-Å crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The α-β sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation

Structural basis for intramembrane proteolysis by rhomboid serine proteases

Intramembrane proteases catalyze peptide bond cleavage of integral membrane protein substrates. This activity is crucial for many biological and pathological processes. Rhomboids are evolutionarily widespread intramembrane serine proteases. Here, we present the 2.3-Å-resolution crystal structure of a rhomboid from Escherichia coli. The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed cavity, which provides a hydrophilic environment for proteolysis. Our results reveal a mechanism to enable water-dependent catalysis at the depth of the hydrophobic milieu of the membrane and suggest how substrates gain access to the sequestered rhomboid active site