How the brain stores a sequence in memory remains largely unknown. We investigated the neural code underlying sequence working memory using two-photon calcium imaging to record thousands of neurons in the prefrontal cortex of macaque monkeys memorizing and then reproducing a sequence of locations after a delay. We discovered a regular geometrical organization: The high-dimensional neural state space during the delay could be decomposed into a sum of low-dimensional subspaces, each storing the spatial location at a given ordinal rank, which could be generalized to novel sequences and explain monkey behavior. The rank subspaces were distributed across large overlapping neural groups, and the integration of ordinal and spatial information occurred at the collective level rather than within single neurons. Thus, a simple representational geometry underlies sequence working memory.
ZnS/ZnO heteronanostructures were prepared to serve as the photoanode of the dye-sensitized solar cells. Two nanostructures, namely, ZnS/ZnO coaxial nanowires and ZnS/ZnO hierarchical nanowires (ZnS nanoparticles on ZnO nanowires), were successfully synthesized by chemical bath deposition and chemical etching processes, respectively. For both of the nanostructures, the ZnS coating can enhance photocurrent and conversion efficiency compared with the bare ZnO nanowires. We propose that ZnS layers in the two nanostructures take effect in different ways in that the ZnS compact layer in the coaxial structure retards the back transfer of electrons to the dye and electrolyte, while the coarse surface of ZnS nanoparticles in the hierarchical nanowires significantly enhances the adsorption of dye molecules. Hence, the ideal photoanode structure for high power-conversion efficiency should have both the compact shell layer and the high surface roughness.
Buforin II (BF2) is a histone-derived antimicrobial peptide that causes cell death by translocating across membranes and interacting with nucleic acids. It contains one proline residue critical for its function. Previous research found that mutations replacing proline lead to decreased membrane translocation and antimicrobial activity as well as increased membrane permeabilization. This study further investigates the role of proline in BF2’s antimicrobial mechanism by considering the effect of changing proline position on membrane translocation, membrane permeabilization, and antimicrobial activity. For this purpose, four mutants were made with proline substitution (P11A) or relocation (P11A/G7P, P11A/V12P, P11A/V15P). These mutations altered the amount of α-helical content. Although antimicrobial activity correlated with the α-helical content for the peptides containing proline, membrane translocation did not. This observation suggests that factors in BF2’s bactericidal mechanism other than translocation must be altered by these mutations. To better explain these trends we also measured the nucleic acid binding and membrane permeabilization of the mutant peptides. A comparison of mutant and wild type BF2 activity revealed that BF2 relies principally on membrane translocation and nucleic acid binding for antimicrobial activity, although membrane permeabilization may play a secondary role for some BF2 variants. A better understanding of the role of proline in the BF2 antimicrobial mechanism will contribute to the further design and development of BF2 analogues. Moreover, since proline residues are prevalent among other antimicrobial peptides, this systematic characterization of BF2 provides general insights that can promote our understanding of other systems.
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