RESUMEN
The demand for polymer composite solutions in bipolar plates for polymer electrolyte membrane fuel cells (PEMFCs) has risen due to advantages over metal plates such as longer lifetime, weight reduction, corrosion resistance, flexible manufacturing, freedom of design, and cost-effectiveness. The challenge with polymer composites is achieving both sufficient electrical conductivity and mechanical stability with high filler content. A carbon fiber fleece as reinforcement in a graphite-filled polypropylene (PP) matrix was investigated for use as bipolar plate material with increased mechanical and sufficient conductive properties. Plates with a thickness of 1 mm containing four layers of fleece impregnated in the PP-graphite compound were produced in a compression molding process. Particle and fiber interactions were investigated via microscopy. The plates were characterized with respect to the electrical conductivity and mechanical stability. High electric conductivity was reached for fiber-reinforced and plain PP-graphite compound plates, with increased filler content leading to a higher conductivity. The contact resistance remained largely unaffected by surface etching as no polymeric skin layer formed during compression molding. Fiber-reinforced plates exhibit twice the tensile strength, a significantly higher tensile modulus, and an increased elongation at break, compared to PP filled only with graphite.
RESUMEN
Pentatricopeptide repeat (PPR) proteins with an E domain have been identified as specific factors for C to U RNA editing in plant organelles. These PPR proteins bind to a unique sequence motif 5' of their target editing sites. Recently, involvement of a combinatorial amino acid code in the P (normal length) and S type (short) PPR domains in sequence specific RNA binding was reported. PPR proteins involved in RNA editing, however, contain not only P and S motifs but also their long variants L (long) and L2 (long2) and the S2 (short2) motifs. We now find that inclusion of these motifs improves the prediction of RNA editing target sites. Previously overlooked RNA editing target sites are suggested from the PPR motif structures of known E-class PPR proteins and are experimentally verified. RNA editing target sites are assigned for the novel PPR protein MEF32 (mitochondrial editing factor 32) and are confirmed in the cDNA.
