Note: When clicking on a Digital Object Identifier (DOI) number, you will be taken to an external site maintained by the publisher.
Some full text articles may not yet be available without a charge during the embargo (administrative interval).
What is a DOI Number?
Some links on this page may take you to non-federal websites. Their policies may differ from this site.
-
The rippled β-sheet is a peptidic structural motif related to but distinct from the pleated β-sheet. Both motifs were predicted in the 1950s by Pauling and Corey. The pleated β-sheet was since observed in countless proteins and peptides and is considered common textbook knowledge. Conversely, the rippled β-sheet only gained a meaningful experimental foundation in the past decade, and the first crystal structural study of rippled β-sheets was published as recently as this year. Noteworthy, the crystallized assembly stopped at the rippled β-dimer stage. It did not form the extended, periodic rippled β-sheet layer topography hypothesized by Pauling and Corey, thus calling the validity of their prediction into question. NMR work conducted since moreover shows that certain model peptides rather form pleated and not rippled β-sheets in solution. To determine whether the periodic rippled β-sheet layer configuration is viable, the field urgently needs crystal structures. Here we report on crystal structures of two racemic and one quasi-racemic aggregating peptide systems, all of which yield periodic rippled antiparallel β-sheet layers that are in excellent agreement with the predictions by Pauling and Corey. Our study establishes the rippled β-sheet layer configuration as a motif with general features and opens the road to structure-based design of unique supramolecular architectures.more » « less
-
Abstract Sample return capsules (SRCs) entering Earth’s atmosphere at hypervelocity from interplanetary space are a valuable resource for studying meteor phenomena. The 2023 September 24 arrival of the Origins, Spectral Interpretation, Resource Identification, and Security-Regolith Explorer SRC provided an unprecedented chance for geophysical observations of a well-characterized source with known parameters, including timing and trajectory. A collaborative effort involving researchers from 16 institutions executed a carefully planned geophysical observational campaign at strategically chosen locations, deploying over 400 ground-based sensors encompassing infrasound, seismic, distributed acoustic sensing, and Global Positioning System technologies. Additionally, balloons equipped with infrasound sensors were launched to capture signals at higher altitudes. This campaign (the largest of its kind so far) yielded a wealth of invaluable data anticipated to fuel scientific inquiry for years to come. The success of the observational campaign is evidenced by the near-universal detection of signals across instruments, both proximal and distal. This paper presents a comprehensive overview of the collective scientific effort, field deployment, and preliminary findings. The early findings have the potential to inform future space missions and terrestrial campaigns, contributing to our understanding of meteoroid interactions with planetary atmospheres. Furthermore, the data set collected during this campaign will improve entry and propagation models and augment the study of atmospheric dynamics and shock phenomena generated by meteoroids and similar sources.more » « less
-
Proteins are commonly known to transfer electrons over distances limited to a few nanometers. However, many biological processes require electron transport over far longer distances. For example, soil and sediment bacteria transport electrons, over hundreds of micrometers to even centimeters, via putative filamentous proteins rich in aromatic residues. However, measurements of true protein conductivity have been hampered by artifacts due to large contact resistances between proteins and electrodes. Using individual amyloid protein crystals with atomic-resolution structures as a model system, we perform contact-free measurements of intrinsic electronic conductivity using a four-electrode approach. We find hole transport through micrometer-long stacked tyrosines at physiologically relevant potentials. Notably, the transport rate through tyrosines (105s−1) is comparable to cytochromes. Our studies therefore show that amyloid proteins can efficiently transport charges, under ordinary thermal conditions, without any need for redox-active metal cofactors, large driving force, or photosensitizers to generate a high oxidation state for charge injection. By measuring conductivity as a function of molecular length, voltage, and temperature, while eliminating the dominant contribution of contact resistances, we show that a multistep hopping mechanism (composed of multiple tunneling steps), not single-step tunneling, explains the measured conductivity. Combined experimental and computational studies reveal that proton-coupled electron transfer confers conductivity; both the energetics of the proton acceptor, a neighboring glutamine, and its proximity to tyrosine influence the hole transport rate through a proton rocking mechanism. Surprisingly, conductivity increases 200-fold upon cooling due to higher availability of the proton acceptor by increased hydrogen bonding.more » « less
An official website of the United States government
