A Thermodynamic Performance Analysis of Triple Effect Vapour Absorption Refrigeration System Using LiBr-H2O

Being an eco-friendly system and a cheaper way to produce cooling effect absorption refrigeration system (ARS) is becoming more popular as it can produce higher cooling capacity than vapor compression refrigeration systems, and it can be powered by other sources of energy (like waste heat from gas and steam turbines, or can utilizes renewable source of heat by sun, geothermal, biomass) other than electricity. In the recent years, the interest in absorption refrigeration system is growing because these systems have environmentally friendly refrigerant and absorbent pairs. In this study, a detail energetic analysis of triple stage LiBr-H20 absorption system using First law of thermodynamics is done. An Energy Equation Solver code are used to simulate the computer program is developed for the cycle and results are validated with past studies available is also done. Mass, energy and exergy balance equations and the various complementary relations constitute the simulation model of the triple effect refrigeration system. Further, the effect of exit temperature of generator, absorber, condenser and evaporator on COP, solution concentration and other parameters are studied. It was found in the study that COP increases with increasing the generator exit temperature keeping the absorber exit temperature constant but when the absorber exit temperature is increased COP tends to decrease and the concentration of weak solution leaving HP generator (Xw3), MP generator (Xw2) and LP generator (Xw1) also increases with increase in generator exit temperature, while it decreases with increase in condenser exit temperature. Keywords: Absorption Refrigeration System (ARS), LiBr + H2O, COP, solution concentration, Energy Equation Solver code, energetic analysis, triple effect refrigeration system.

Structural and energetic analysis of metastable intermediate states in the E1P–E2P transition of Ca2+-ATPase

Sarcoplasmic reticulum (SR) Ca2+-ATPase transports two Ca2+ ions from the cytoplasm to the SR lumen against a large concentration gradient. X-ray crystallography has revealed the atomic structures of the protein before and after the dissociation of Ca2+, while biochemical studies have suggested the existence of intermediate states in the transition between E1P⋅ADP⋅2Ca2+ and E2P. Here, we explore the pathway and free energy profile of the transition using atomistic molecular dynamics simulations with the mean-force string method and umbrella sampling. The simulations suggest that a series of structural changes accompany the ordered dissociation of ADP, the A-domain rotation, and the rearrangement of the transmembrane (TM) helices. The luminal gate then opens to release Ca2+ ions toward the SR lumen. Intermediate structures on the pathway are stabilized by transient sidechain interactions between the A- and P-domains. Lipid molecules between TM helices play a key role in the stabilization. Free energy profiles of the transition assuming different protonation states suggest rapid exchanges between Ca2+ ions and protons when the Ca2+ ions are released toward the SR lumen.

Human responses to the Ilopango Tierra Blanca Joven eruption: excavations at San Andrés, El Salvador

Human responses to catastrophic natural events form an important research theme in archaeology. Using excavation and radiocarbon data, this article investigates the socio-cultural impact of the mid-first-millennium AD Tierra Blanca Joven eruption at San Andrés, El Salvador. The data, along with an architectural energetic analysis of the Campana structure at San Andrés, indicate that survivors and/or re-settlers made considerable efforts to construct monumental public buildings immediately following the eruption, using large quantities of volcanic tephra as construction material. Such re-building played important religious, social and political roles in human responses to the eruption. The study contributes to discussions about human creativity, adaptation and resilience in the face of abrupt environmental change.

Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin

The Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) genome is evolving as the viral pandemic continues its active phase around the world. The Papain-like protease (PLpro) is a domain of Nsp3 – a large multi-domain protein that is an essential component of the replication-transcription complex, making it a good therapeutic target. PLpro is a multi-functional protein encoded in coronaviruses that can cleave viral polyproteins, poly-ubiquitin and protective Interferon Stimulated Gene 15 product, ISG15, which mimics a head-to-tail linked ubiquitin (Ub) dimer. PLpro across coronavirus families showed divergent selectivity for recognition and cleavage of these protein substrates despite sequence conservation. However, it is not clear how sequence changes in SARS-CoV-2 PLpro alter its selectivity for substrates and what outcome this has on the pathogenesis of the virus. We show that SARS-CoV-2 PLpro preferentially binds ISG15 over Ub and K48-linked Ub2. We determined crystal structures of PLpro in complex with human K48-Ub2 and ISG15 revealing that dual domain recognition of ISG15 drives substrate selectivity over Ub and Ub2. We also characterized the PLpro substrate interactions using solution NMR, cross-linking mass spectrometry to support that ISG15 is recognized via two domains while Ub2 binds primarily through one Ub domain. Finally, energetic analysis of the binding interfaces between PLpro from SARS-CoV-1 and SARS-CoV-2 with ISG15 and Ub2 define the sequence determinants for how PLpros from different coronaviruses recognize two topologically distinct substrates and how evolution of the protease altered its substrate selectivity. Our work reveals how PLpro substrate selectivity may evolve in PLpro coronaviruses variants enabling design of more effective therapeutics.