Micro-channel development and hydrogen adsorption properties in templated microporous carbons containing platinum nanoparticles

Ordered microporous carbons containing dispersed platinum nanoparticles were fabricated and chosen as suitable models to investigate micro-structure development and hydrogen transport properties of zeolite-templated carbons. X-ray photoelectron spectroscopy analysis revealed that the enhanced heat of adsorption is related to the narrow micro-channels templated from the zeolite and the presence of certain CO groups on the carbon. The lack of a well-defined and intense rotational transition line and the persistent broad H₂ recoil spectrum in neutron scattering results suggests a distribution of binding sites. Most interestingly, hydrogen diffusion occurs on two time scales, consisting of a fast liquid-like jump diffusion on the timescale of picoseconds along with an even faster bulk-like diffusion. The liquid-like motion is characterized by a diffusion constant of (2.1 ± 0.3) × 10⁻⁸ m²/s with an activation energy of ca. 77 K; both values indicate somewhat lower mobility than similar dynamics of H₂ on nanotubes, activated carbon XC-72, or Grafoil, yet greater mobility than that of bulk liquid. These unusual characteristics for hydrogen in carbons are believed to arise from the network of narrow pores in this zeolite-templated image of the zeolite. In fact, the diffusion constants of the templated carbons are extremely similar to those measured for zeolite 13X.     

Enhancing β3 -peptide bundle stability by design

We reported recently that certain β(3) -peptides self-assemble in aqueous solution into discrete bundles of unique structure and defined stoichiometry. The first β-peptide bundle reported was the octameric Zwit-1F, whose fold is characterized by a well-packed, leucine-rich core and a salt-bridge-rich surface. Close inspection of the Zwit-1F structure revealed four nonideal interhelical salt-bridge interactions whose heavy atom-heavy atom distances were longer than found in natural proteins of known structure. Here we demonstrate that the thermodynamic stability of a β-peptide bundle can be enhanced by optimizing the length of these four interhelical salt bridges. Combined with previous work on the role of internal packing residues, these results provide another critical step in the "bottom-up" formation of β-peptide assemblies with defined sizes, reproducible structures, and sophisticated function.     

National-scale implementation of mandatory freshwater farm plans: a mechanism to deliver water quality improvement in productive catchments in New Zealand?

Nutrient Cycling in Agroecosystems - Reducing agriculturally derived diffuse contaminant losses (via non-point sources) from land to water has proven difficult for decades. Owing to the diversity...