RESUMO
A series of liquid crystalline porphyrins was synthesized, purified, and characterized. Differential scanning calorimetry (DSC) and hot-stage polarized optical microscopy (HS-POM) revealed that the porphyrins in the series with shorter alkyl arm lengths exhibit kinetic cold crystallization, wherein the molecules spontaneously organize into large, disc-like structures that remain stable upon cooling. Using DSC, the kinetic and thermodynamic parameters related to these materials were determined. Analysis of non-isothermal crystallization revealed the presence of multiple nucleation and growth processes related to cold crystallization.
RESUMO
Canonical processing of miRNA begins in the nucleus with the Microprocessor complex, which is minimally composed of the RNase III enzyme Drosha and two copies of its cofactor protein DGCR8. In structural analogy to most RNase III enzymes, Drosha possesses a modular domain with the double-stranded RNA binding domain (dsRBD) fold. Unlike the dsRBDs found in most members of the RNase III family, the Drosha-dsRBD does not display double-stranded RNA binding activity; perhaps related to this, the Drosha-dsRBD amino acid sequence does not conform well to the canonical patterns expected for a dsRBD. In this article, we investigate the impact on miRNA processing of engineering double-stranded RNA binding activity into Drosha's non-canonical dsRBD. Our findings corroborate previous studies that have demonstrated the Drosha-dsRBD is necessary for miRNA processing and suggest that the amino acid composition in the second α-helix of the domain is critical to support its evolved function.
