Revisiting the Ω(2012)\Omega(2012) as a hadronic molecule and its strong decays

Recently, the Belle collaboration measured the ratios of the branching fractions of the newly observed $\Omega(2012)$ excited state. They did not observe significant signals for the $\Omega(2012) \to \bar{K} \Xi^*(1530) \to \bar{K} \pi \Xi$ decay, and reported an upper limit for the ratio of the three body decay to the two body decay mode of $\Omega(2012) \to \bar{K} \Xi$. In this work, we revisit the newly observed $\Omega(2012)$ from the molecular perspective where this resonance appears to be a dynamically generated state with spin-parity $3/2^-$ from the coupled channels interactions of the $\bar{K} \Xi^*(1530)$ and $\eta \Omega$ in $s$-wave and $\bar{K} \Xi$ in $d$-wave. With the model parameters for the $d$-wave interaction, we show that the ratio of these decay fractions reported recently by the Belle collaboration can be easily accommodated.Comment: Published version. Published in Eur.\ Phys.\ J.\ C {\bf 80}, 361 (2020

A New Role for the CYT-18 N-Terminus and Three-Dimensional DNA Crystals as Vehicles for Biocatalysis

The bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (N. crassa mt TyrRS; CYT-18 protein) promotes the splicing of multiple group I introns by stabilizing the catalytically active intron structures. CYT-18, and mt TyrRS's from related fungal species, have evolved to promote group I intron splicing partly by accumulation of three N-terminal domain insertions that create a structure-stabilizing scaffold for critical tertiary interactions between the two major group I intron domains. The primarily alpha-helical N-terminal insertion, H0, contributes to protein stability and is necessary for splicing the N. crassa ND1 intron, but is dispensable for splicing the N. crassa mt LSU intron. Herein, I show CYT-18 with a complete H0 deletion retains residual ND1 intron splicing activity and addition of the missing N-terminus in trans restores a significant portion of its splicing activity. This peptide complementation assay revealed important characteristics of the CYT-18/group I intron interaction including the stoichiometry of H0 in intron splicing and the importance of specific H0 residues. Evaluation of truncated H0 peptides in this assay also suggests a previously unknown structural role of the first five N-terminal residues of CYT-18. These residues interact directly with another splicing insertion, making H0 a central structural element responsible for connecting all three N-terminal splicing insertions. Transitioning to a separate study, I have demonstrated that enzymes retain catalytic activity when captured in the solvent channels of three-dimensional (3D) DNA crystals. Using RNase A as a model enzyme system this work shows that crystals infused with enzyme can cleave a fluorescent dinucleotide substrate with similar kinetic restrictions as other immobilized enzyme systems, mainly limited by diffusion of substrate. This new vehicle for immobilized enzymes, created entirely from biomolecules, provides a platform for developing modular solid-state catalysts that could be both biocompatible and biodegradable

4-Methyl-N-[(Z)-3-(4-methyl­phen­ylsulfon­yl)-1,3-thia­zolidin-2-yl­idene]benzene­sulfonamide

In the crystal structure of the title compound, C17H18N2O4S3, mol­ecules are connected into centrosymmetric dimers via weak inter­molecular C—H⋯π inter­actions. These dimers are further connected through a series of weak C—H⋯O hydrogen bonds, while futher C—H⋯π inter­actions involving the phenyl and thia­zoline rings are also observed. The thia­zolidine ring is twisted from the benzene rings rings by dihedral angles of 79.1 (1) and 85.0 (1)°, while the dihedral angle between two benzene rings is 76.0 (1)°