Coating Distribution Analysis on Gas Diffusion Layers for Polymer Electrolyte Fuel Cells by Neutron and X-ray High-Resolution Tomography.

Coating load and distribution in gas diffusion layers (GDLs) for polymer electrolyte fuel cells (PEFCs) have a major influence on mass transport losses. To be able to optimize the coating distribution and get more accurate data about the influence of the coating on the PEFC performance, better characterization techniques are necessary. Common analysis techniques are limited to selected sections of the material, or they are not sensitive to small amounts of coating. We propose a new methodology to get a complete description of the coating distribution and the GDL structure by combining high-resolution X-ray tomography with high-resolution neutron tomography. Using an isotopic gadolinium staining method to enhance the neutron and X-ray absorption contrast, lower quantities of coating can be detected. The combination of both imaging techniques allows for a more detailed analysis of the coating distribution.

pH-jump induced leucine zipper folding beyond the diffusion limit.

The folding of a pH-sensitive leucine zipper, that is, a GCN4 mutant containing eight glutamic acid residues, has been investigated. A pH-jump induced by a caged proton (o-nitrobenzaldehyde, oNBA) is employed to initiate the process, and time-resolved IR spectroscopy of the amide I band is used to probe it. The experiment has been carefully designed to minimize the buffer capacity of the sample solution so that a large pH jump can be achieved, leading to a transition from a completely unfolded to a completely folded state with a single laser shot. In order to eliminate the otherwise rate-limiting diffusion-controlled step of the association of two peptides, they have been covalently linked. The results for the folding kinetics of the cross-linked peptide are compared with those of an unlinked peptide, which reveals a detailed picture of the folding mechanism. That is, folding occurs in two steps, one on an ∼1-2 µs time scale leading to a partially folded α-helix even in the monomeric case and a second one leading to the final coiled-coil structure on distinctively different time scales of ∼30 µs for the cross-linked peptide and ∼200 µs for the unlinked peptide. By varying the initial pH, it is found that the folding mechanism is consistent with a thermodynamic two-state model, despite the fact that a transient intermediate is observed in the kinetic experiment.