Publications by authors named "J J De Yoreo"

Biological organisms engineer peptide sequences to fold into membrane pore proteins capable of performing a wide variety of transport functions. Synthetic de novo-designed membrane pores can mimic this approach to achieve a potentially even larger set of functions. Here we explore water, solute, and ion transport in three de novo designed β-barrel membrane channels in the 5-10 Å pore size range.

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Understanding defect healing is necessary to control the electronic and optoelectronic performance of devices based on nanoparticle (NP) superlattices. However, a key challenge remains to understand how NP interactions and the resulting dynamics are coupled to defect self-elimination during assembly processes. Additional degrees of freedom that account for the anisotropic nature of NPs associated with rotational dynamics and torques further complicate the challenge.

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The extensive deposits of calcium carbonate (CaCO) generated by marine organisms constitute the largest and oldest carbon dioxide (CO) reservoir. These organisms utilize macromolecules like peptides and proteins to facilitate the nucleation and growth of carbonate minerals, serving as an effective method for CO sequestration. However, the precise mechanisms behind this process remain elusive.

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Metal carbonates, which are ubiquitous in the near-surface mineral record, are a major product of biomineralizing organisms and serve as important targets for capturing anthropogenic CO emissions. However, pathways of carbonate mineralization typically diverge from classical predictions due to the involvement of disordered precursors, such as the dense liquid phase (DLP), yet little is known about DLP formation or solidification processes. Using in situ methods we report that a highly hydrated bicarbonate DLP forms via liquid-liquid phase separation and transforms into hollow hydrated amorphous CaCO particles.

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Despite the promise of silk-based devices, the inherent disorder of native silk limits performance. Here, we report highly ordered two-dimensional silk fibroin (SF) films grown epitaxially on van der Waals (vdW) substrates. Using atomic force microscopy, nano-Fourier transform infrared spectroscopy, and molecular dynamics, we show that the films consist of lamellae of SF molecules that exhibit the same secondary structure as the nanocrystallites of native silk.

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