Towards Continuous Production of Shaped Honeycombs

Honeycomb sandwich panels are widely used for high performance parts subject to bending loads, but their manufacturing costs remain high. In particular, for parts with non-flat, non-uniform geometry, honeycombs must be machined or thermoformed with great care and expense. The ability to produce shaped honeycombs would allow sandwich panels to replace monolithic parts in a number of high performance, space-constrained applications, while also providing new areas of research for structural optimization, distributed sensing and actuation, and on-site production of infrastructure. Previous work has shown methods of directly producing shaped honeycombs by cutting and folding flat sheets of material. This research extends these methods by demonstrating work towards a continuous process for the cutting and folding steps of this process. An algorithm for producing a manufacturable cut-and-fold pattern from a three-dimensional volume is designed, and a machine for automatically performing the required cutting and parallel folding is proposed and prototyped. The accuracy of the creases placed by this machine is characterized and the impact of creasing order is demonstrated. Finally, a prototype part is produced and future work is sketched towards full process automation.

Toward a quantitative description of microscopic pathway heterogeneity in protein folding

Experimentally consistent statistical modeling of protein folding thermodynamics reveals unprecedented complexity with numerous parallel folding routes in five different proteins.

Disorder drives cooperative folding in a multidomain protein

Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function—for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding.

Parallel folding topology-selective label-free detection and monitoring of conformational and topological changes of different G-quadruplex DNAs by emission spectral changes via FRET of mPPE-Ala–Pt(ii) complex ensemble

The ensemble of platinum(ii) complex andmPPE-Ala has been demonstrated for label-free detection of G-quadruplex DNAs and the probing of their topological transitions.