Thermodynamic and kinetic analysis of the LAO binding protein and its isolated domains reveal non-additivity in stability, folding and function.

Substrate-binding proteins (SBPs) are used by organisms from the three domains of life for transport and signalling. SBPs are composed of two domains that collectively trap ligands with high affinity and selectivity. To explore the role of the domains and the integrity of the hinge region between them in the function and conformation of SBPs, here, we describe the ligand binding, conformational stability and folding kinetics of the Lysine Arginine Ornithine (LAO) binding protein from Salmonella thiphimurium and constructs corresponding to its two independent domains.

De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2.

We developed a de novo protein design strategy to swiftly engineer decoys for neutralizing pathogens that exploit extracellular host proteins to infect the cell. Our pipeline allowed the design, validation, and optimization of de novo human angiotensin-converting enzyme 2 (hACE2) decoys to neutralize severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The best monovalent decoy, CTC-445.

design of ACE2 protein decoys to neutralize SARS-CoV-2.

There is an urgent need for the ability to rapidly develop effective countermeasures for emerging biological threats, such as the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that causes the ongoing coronavirus disease 2019 (COVID-19) pandemic. We have developed a generalized computational design strategy to rapidly engineer proteins that precisely recapitulate the protein surface targeted by biological agents, like viruses, to gain entry into cells. The designed proteins act as decoys that block cellular entry and aim to be resilient to viral mutational escape.

Crystal structure of (NH4)2[Fe(II) 5(HPO3)6], a new open-framework phosphite.

Di-ammonium hexa-phosphito-penta-ferrate(II), (NH4)2[Fe5(HPO3)6], was synthesized under mild hydro-thermal conditions and autogeneous pressure, yielding twinned crystals. The crystal structure exhibits an [Fe(II) 5(HPO3)6](2-) open framework with NH4 (+) groups as counter-cations. The anionic skeleton is based on (001) sheets of [FeO6] octa-hedra (one with point-group symmetry 3.

Catalytic performance of the high and low temperature polymorphs of (C6N2H16)0.5[(VO)(HAsO4)F]: structural, thermal, spectroscopic and magnetic studies.

(C(6)N(2)H(16))(0.5)[(VO)(HAsO(4))F] 1 has been synthesized using mild hydrothermal conditions under autogenous pressure. Above 70 degrees C, this phase has a polymorph with the same chemical composition 2 in which the organic 1,4-diamincyclohexane molecule adopts a different conformation.