Fold Structures Research Articles

Transpressional inversion and fold superimposition in the Southern Eastern Desert of Egypt, East African Orogenic Belt

Transpressional deformation has played a key role in the development of the East African Orogenic Belt and the Arabian-Nubian Shield during the Neoproterozoic. This study examines the folding structures in the Kharit shear zone in the southern Eastern Desert of Egypt. This work aims to investigate the relationship between the development of large-scale folds and the mechanism of transpressional inversion within the Kharit shear zone. The structural analysis reveals the occurrence of extensive folds formed through three generations of folding and their associated fabrics. The F1 folds developed during an early phase of north-south shortening, while the F2 folds, distinguished by their overturned and doubly plunging forms, are associated with dextral transpressional deformation along the Kharit shear zone. The subsequent F3 folds, in contrast, are indicative of sinistral transpressional shearing, implying a transpressional inversion that evolves from pure shear to increasingly intricate patterns of fold interference throughout the shear zone. Regionally, the interference pattern changes from west to east, transitioning from lobate-cuspate shapes to mushroom shapes and then to crescent shapes. The refolding of map-scale northeast-trending folds by northwest- and west-northwest-trending folds leads to the formation of this fold interference structure. Transpressional shear systems rework and reactivate the rocks along opposing kinematic planes. This shear-sense reversal emerged from the oblique convergence of East and West Gondwana, coinciding with the activity of the Najd Fault System between 620 and 540 Ma.

Unraveling the Molecular Architecture of Mosquito D1-Like Dopamine Receptors: Insights Into Ligand Binding and Structural Dynamics for Insecticide Development.

Vector-borne diseases pose a severe threat to human life, contributing significantly to global mortality. Understanding the structure-function relationship of the vector proteins is pivotal for effective insecticide development due to their involvement in drug resistance and disease transmission. This study reports the structural and dynamic features of D1-like dopamine receptors (DARs) in disease-causing mosquito species, such as Aedes aegypti, Culex quinquefasciatus, Anopheles gambiae, and Anopheles stephensi. Through molecular modeling and simulations, we describe the common structural fold of mosquito DARs within the G-protein-coupled receptor family, highlighting the importance of an orthosteric and enlarged binding pocket. The orthosteric binding pocket, resembling a cage-like structure, is situated ~15 Å deep within the protein, with two serine residues forming the roof and an aspartate residue, along with two conserved water molecules (W1 and W2), forming the floor. The side walls are composed of two phenylalanine residues on one side and a valine residue on the other. The antagonist binding site, an enlarged binding pocket (EBP) near the entrance cavity, can accommodate ligands of varying sizes. The binding energy of dopamine is observed to be ~2-3 kcal/mol higher than that of the antagonist molecules amitriptyline, asenapine, and flupenthixol in mosquito DARs. These antagonist molecules bind to EBP, which obstructs dopamine movement toward the active site, thereby inhibiting signal transduction. Our findings elucidate the molecular architecture of the binding pockets and the versatility of DARs in accommodating diverse ligands, providing a foundational framework for future drug and insecticide development.

Ig or Not Ig? That Is the Question: The Nucleating Supersecondary Structure of the Ig-Fold and the Extended Ig Universe.

Observing the omnipresence of the Ig-fold in all domains of life, one may wonder why this fold among all is such a wunderkind of evolution. Culminating in vertebrates, it enables a myriad of functions at the heart of the immune, nervous, vascular, and muscular systems. We suggest the Ig-fold resilience lies in the robust folding of a core supersecondary structure (SSS) that can accommodate a myriad of topological variations. In this chapter, we focus on the core supersecondary structure common to all topostructural variants of the Ig-fold and will see that this pattern can also be found in other β-sandwich folds. It represents a highly resilient central SSS that accommodates a very high plasticity observed among β-sandwiches. We have recently developed a universal numbering system to identify and annotate Ig-domains, Ig-like domains, and what we now call Ig-extended domains, i.e., β-sandwiches that contain and extend the Ig-fold topology (to be published). A universal numbering scheme, common to all topological and structural variants of any domain sharing the Ig-fold, allows a direct comparison of any Ig, Ig-like, and Ig-extended domain in sequence, topology, and structure. This can therefore help understand the robust patterns in Ig-folding and interactions with other Ig or non-Ig proteins, as well as help trace evolutionary patterns of immunoglobulin domains. The universal numbering scheme, called IgStrand, is now at the heart of an algorithm that can label secondary structure elements of the Ig-fold for any topological variant. It is implemented in the open-source web-based iCn3D program from NCBI (Wang, Youkharibache, Zhang, Lanczycki, Geer, Madej, Phan, Ward, Lu, Marchler, Bioinformatics 36:131-135, 2020). Interestingly, that algorithm captures SSS homologies across a very large spectrum of β-sandwiches, and one can envision classifying numerous such sandwiches as "Ig-extended" domains and their variable topological arrangements. In this chapter, we go through examples of Ig, Ig-like, and Ig-extended domains as in a journey through cells: in the cell nucleus, in the cytoplasm, or on extracellular regions of cell surface receptors, and in viruses.

Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions.

Enzymatic proteolysis is the key process to produce bioavailable nitrogen in natural terrestrial and aquatic ecosystems for microorganisms and plants. However, little is known on how protein degradation is influenced by organic contaminants. As we known, the overuse of organophosphate esters (OPEs) has caused serious pollution in soil, water, and sediment. Thereby we studied the effect of OPEs on the proteolysis of protein GB1 in aqueous system at neutral pH, and explored the underlying molecular mechanism. Colorimetric ninhydrin methods and SDS-PAGE results revealed that OPEs inhibited the enzymatic hydrolysis of protein GB1. Based on fluorescence quenching experiments, the binding constant (LogKA) were found in order: 6.16 (dibutyl phosphate)>5.11 (diethyl phosphate)>1.78 (tributyl phosphate)>0.876 (triethyl phosphate), proving the interactions between OPEs and protein GB1. Further spectroscopic experiments and molecular docking simulations showed that OPEs could entered the pocket structure of GB1 and induced secondary structural changes and protein folding through non-covalent interactions dominated by hydrogen bonding and van der Waals forces. In addition, organophosphate diesters (di-OPEs) and long-chain OPEs had stronger affinity to GB1, due to the more negative and denser electrostatic surface potential distributions. The deformation of proteins hindered the contact between their active sites and enzymes, leading to the inhibition of GB1 hydrolysis. This study deepened our understanding of the effect of OPEs on protein transformation and degradation, which could further influence the ecological functions and nutrient cycling.

PSGL-1 excludes HIV Env from virion surface through spatial hindrance involving structural folding of the decameric repeats (DR).

P-selectin glycoprotein ligand-1 (PSGL-1), a mucin-like surface glycoprotein, is primarily expressed on lymphoid and myeloid cells. PSGL-1 has recently been identified as an HIV restriction factor, blocking HIV infectivity mainly through virion incorporation that sterically hinders virion attachment to target cells. PSGL-1 also inhibits HIV Env incorporation into virions. However, the molecular mechanisms of PSGL-1-mediated Env exclusion remained unclear. Here, we investigated the role of PSGL-1's extracellular (EC) and intracellular (IC) domains in Env exclusion. We demonstrate that both EC and IC are important for Env exclusion; when EC was deleted, PSGL-1 completely lost its ability to inhibit Env incorporation, whereas when IC was deleted, PSGL-1 partially lost this activity. In addition, when the decameric repeats (DR) were deleted from EC, PSGL-1 also lost its ability to inhibit Env incorporation. Sequential DR deletion mutagenesis further demonstrated that a minimum of 9 DRs is necessary for Env exclusion. Molecular modeling of the DR structure revealed that PSGL-1 mutants with 7 or fewer DRs pose as an extended "rod-like" structure, whereas those with 9 or more DRs collapse into a "coil-like" structure that spatially excludes Env. Our studies suggest a model in which Env exclusion involves Gag-mediated PSGL-1 targeting to the virion assembly site where DR-mediated spatial exclusion blocks Env incorporation.

Quaternary arrangements of membrane proteins: an aquaporin case.

Integral polytopic α-helical membrane transporters and aquaporins move and distribute various molecules and dispose of or compartmentalize harmful elements that gather in living cells. The view shaped nearly 25 years ago states that integrating these proteins into cellular membranes can be considered a two-stage process, with hydrophobic core folding into α-helices across membranes to form functional entities (Popot and Engelman, 1990; Biochemistry29, 4031-4037). Since then, a large body of evidence cemented the roles of structural properties of membrane proteins and bilayer solvent components in forming functional assemblies. This mini-review updates our understanding of multifaced factors, which underlie transporters integration and oligomerization, focusing on water-permeating aquaporins. This work also elaborates on how individual monomers of bacterial and mammalian aquaporin tetramers, interact with each other, and how tetramers form contacts with lipids after being embedded in lipid bilayers of known composition, which mimics bacterial and mammalian membranes. Although this mini-review describes findings acquired using current methods, the view is open to how to extend this knowledge through, e.g. single-molecule-based and in situ cryogenic-electron tomography techniques. These and other methods could unravel the sources of entropy for membrane protein assemblies and pathways underlying integration, folding, oligomerization and quaternary structure formation with binding partners. We could expect that these exceedingly interdisciplinary approaches will form the basis for creating optimized transport systems, which could inspire bioengineering to develop a sustainable and healthy society.

Age-related remodeling of the vocal fold extracellular matrix composition, structure, and biomechanics during tissue maturation

ABSTRACT Purpose The vocal folds (VFs) are among the most mechanically active connective tissues, vibrating between 80 and 250 hz during speech. Overall VF function is determined by the composition and structure of their extracellular matrix (ECM). During tissue maturation, the VFs remodel from a monolayer of collagen fibers to a tri-layered structure, affecting tissue biomechanics. However, age-related VF ECM remodeling remains poorly understood since few studies have explored the proteins governing collagen fibrillogenesis or the non-collagenous ECM components critical for VF elasticity. Materials and Methods VFs from immature, sexually mature, and skeletally mature rats were evaluated by endoscopy, histology, and electron microscopy for cellular and biochemical composition, ECM organization, and proteoglycan distribution. Nanoindentation modulus was determined by atomic force microscopy. Results Collagen fiber abundance, maturity, and alignment are low in immature rats but show an age-dependent increase during tissue maturation. Lumican and fibromodulin, which regulate early-stage collagen fibril formation, are distributed throughout the VFs, and their abundance decreases with age. Decorin, involved in collagen organization, is concentrated just beneath the epithelium and increases with age. Elastin levels increase during tissue maturation, but hyaluronic acid abundance and distribution remain consistent with age. VF nanoindentation modulus trends toward a decrease with age. Conclusion This work identifies changes in VF ECM composition and organization during tissue maturation, focusing on proteins that regulate collagen fibrillogenesis, fiber assembly, and VF biomechanics. These findings may inform the development of pro-reparative therapies designed to influence collagen network structure and overall ECM dysregulation in a number of laryngeal pathologies.

Unique structural features in a deep-sea CYP51 relate to high pressure adaptation.

Cytochromes P450 (CYP) form one of the largest enzyme superfamilies on Earth, with similar structural fold but biological functions varying from synthesis of physiologically essential compounds to metabolism of myriad xenobiotics. Here we determined the crystal structures of Coryphaenoides armatus and human sterol 14α-demethylases (CYP51s). Both structures reveal elements that imply elevated conformational flexibility, uncovering molecular basis for faster catalytic rates, lower substrate selectivity, and resistance to inhibition. These elements as well as the unique inward/outward location of the FG arm/β4 hairpin in the fish CYP51 structure were not predicted by artificial intelligence molecular modelling. The structural distinction of C. armatus CYP51, which is the first structurally characterized deep-sea P450, suggests stronger involvement of the membrane environment in regulation of this enzyme function. We interpret this as a co-adaptation of membrane protein structure with changes in membrane lipid composition during evolutionary incursion to life in the deep sea.

Comprehensive Analysis and Application Research of Advanced Computational Algorithms in Protein Folding Simulations

Protein engineering stands at the forefront of biotechnology, aiming to modify natural proteins or create new ones tailored to specific functional requirements. The three-dimensional structures of proteins, particularly their folding patterns, are critical in defining their biological roles. Accurate prediction and detailed examination of these protein folding structures are crucial in protein engineering. The close relationship between protein structure and function highlights the importance of understanding protein folding dynamics to successfully manipulate protein designs for intended uses. Genetic algorithms (GA), taking inspiration from natural evolutionary principles, employ a heuristic search approach that integrates elements of randomness. In contrast, simulated annealing (SA) leverages stochastic optimization techniques based on the Monte Carlo method, theoretically capable of approximating the global optimum with a high degree of accuracy. Additionally, generalized ensemble methods are increasingly used to explore protein folding processes. This paper explores the fundamental principles and practical applications of these algorithms in simulating protein folding dynamics, aiming to enhance the methodologies used in protein engineering. This exploration not only aids in the refinement of protein design but also extends the potential applications of engineered proteins in various scientific and industrial fields.

Benzimidazole resistance-associated mutations improve the in silico dimerization of hookworm tubulin: An additional resistance mechanism

Background and Aim: Mutations in the β-tubulin genes of helminths confer benzimidazole (BZ) resistance by reducing the drug’s binding efficiency to the expressed protein. However, the effects of these resistance-associated mutations on tubulin dimer formation in soil-transmitted helminths remain unknown. Therefore, this study aimed to investigate the impact of these mutations on the in silico dimerization of hookworm α- and β-tubulins using open-source bioinformatics tools. Materials and Methods: Using AlphaFold 3, the α- and β-tubulin amino acid sequences of Ancylostoma ceylanicum were used to predict the structural fold of the hookworm tubulin heterodimer. The modeled complexes were subjected to several protein structure quality assurance checks. The binding free energies, overall binding affinity, dissociation constant, and interacting amino acids of the complex were determined. The dimer’s structural flexibility and motion were simulated through molecular dynamics. Results: BZ resistance-associated amino acid substitutions in the β-tubulin isotype 1 protein of hookworms altered tubulin dimerization. The E198K, E198V, and F200Y mutations conferred the strongest and most stable binding between the α and β subunits, surpassing that of the wild-type. In contrast, complexes with the Q134H and F200L mutations exhibited the opposite effect. Molecular dynamics simulations showed that wild-type and mutant tubulin dimers exhibited similar dynamic behavior, with slight deviations in those carrying the F200L and E198K mutations. Conclusion: Resistance-associated mutations in hookworms impair BZ binding to β-tubulin and enhance tubulin dimer interactions, thereby increasing the parasite’s ability to withstand treatment. Conversely, other mutations weaken these interactions, potentially compromising hookworm viability. These findings offer novel insights into helminth tubulin dimerization and provide a valuable foundation for developing anthelmintics targeting this crucial biological process. Keywords: Ancylostoma, anthelmintic resistance, microtubules, soil-transmitted helminths.

Thermodynamic and Conformational Analysis of GTRNase and Lysozyme Proteins Under Thermal Variations using Molecular Dynamics Simulations

This study examines the thermodynamic and conformational dynamics of GTRNase and lysozyme proteins under varying temperature conditions using molecular dynamics (MD) simulations. The objective is to evaluate their structural stability, folding behavior, and thermodynamic properties to understand their responses to thermal fluctuations. Protein structures were retrieved from the Protein Data Bank (PDB), refined to remove extraneous molecules, and simulated using GROMACS 2022.2 under NVT and NPT ensembles, spanning temperatures from 270 K to 380 K. The results revealed distinct behaviors for the two proteins. GTRNase exhibited a slight escalation in radius of gyration (Rg) from 1.434 nm at 270 K to 1.445 nm at 380 K, suggesting a marginal conformational expansion. In contrast, lysozyme maintained a consistent Rg of 1.38 nm over the same temperature range, indicating structural compactness. Root mean square deviation (RMSD) data demonstrated increased flexibility in both proteins, with GTRNase escalating from 0.115 nm at 270 K to 0.179 nm at 380 K and lysozyme rising from 0.102 nm to 0.142 nm across the temperature range. Solvent-accessible surface area (SASA) for GTRNase fluctuated between 69 nm² and 73 nm², with the lowest value observed at 300 K and the highest at 370 K. These findings highlight that GTRNase is more susceptible to thermal perturbations than lysozyme, showing greater conformational flexibility and expansion. This research underscores the utility of MD simulations in exploring protein behavior and provides valuable insights for applications in protein engineering and drug design.

Structural Evaluation of Interleukin-19 Cytokine and Interleukin-19-Bound Receptor Complex Using Computational Immuno-Engineering Approach

Interleukin 19 (IL-19) is an anti-inflammatory cytokine that belongs to the IL-10 family, where IL-20 and IL-24 also exist. While IL-19 and IL-20 share some comparable structural folds, there are certain structural divergences in their N-terminal ends. To date, there are no reported IL-19 receptors; although, it has been suggested in the literature that IL-19 would bind to lL-20 receptor (IL-20R) and trigger the JAK-STAT signaling pathways. The present report examines the structure of the IL-19 cytokine and its receptor complex using a computational approach. Specifically, the postulated modes of interactions for IL-20R as an IL-19 receptor are examined on the basis of a set of computational findings. The author has used molecular docking and molecular dynamics simulation to generate a 3D model for the IL-19 complex with IL-20R. When a protein’s crystal structure is not available in the literature, predictive modeling is often employed to determine the protein’s 3D structure. The model assessment can be based on various factors, which include stability analysis using RMSD calculations, tracking changes in time-based secondary structures and the associated Gibbs energies, ΔG. Since one model complex (referred to as model A throughout this paper) can be used as a working hypothesis for future experiments, this structure has been explored here in detail to check its stability, subunit interfaces, and binding residues. The information gathered in this approach can potentially help to design specific experiments to test the validity of the model protein structure. Additionally, the results of this research should be relevant for understanding anti-inflammatory mechanisms and, eventually, could contribute to the efforts for therapeutic developments and targeted therapy.

Revealing the correlation between asymmetric structure and low thermal conductivity in Janus-graphene via machine learning force constant potential

Understanding the fundamental link between structure and functionalization is crucial for designing and optimizing functional materials, since different structural configurations could trigger materials to demonstrate diverse physical and chemical properties. However, the correlation between crystal structure and thermal conductivity (κ) remains unclear. In this study, taking two-dimensional (2D) carbon allotropes Janus-graphene and graphene as study cases, we utilize phonon Boltzmann transport equation combined with machine learning potential to thoroughly investigate the complex folding structure of pure sp2 hybridized Janus-graphene from the perspective of crystal structure, phonon modal resolved thermal transport, and atomic interactions, with the goal of identifying the underlying relationship between 2D geometry and κ. The results reveal that the folded structure in Janus-graphene causes strong symmetry breaking, significantly reduces phonon group velocities, increases phonon–phonon scattering, and ultimately leads to low κ. These findings enhance our understanding of how atomic structure folding affects thermal transport and the relationship between structure and functionalization.

High fitness paths can connect proteins with low sequence overlap.

The structure and function of a protein are determined by its amino acid sequence. While random mutations change a protein's sequence, evolutionary forces shape its structural fold and biological activity. Studies have shown that neutral networks can connect a local region of sequence space by single residue mutations that preserve viability. However, the larger-scale connectedness of protein morphospace remains poorly understood. Recent advances in artificial intelligence have enabled us to computationally predict a protein's structure and quantify its functional plausibility. Here we build on these tools to develop an algorithm that generates viable paths between distantly related extant protein pairs. The intermediate sequences in these paths differ by single residue changes over subsequent steps - substitutions, insertions and deletions are admissible moves. Their fitness is evaluated using the protein language model ESM2, and maintained as high as possible subject to the constraints of the traversal. We document the qualitative variation across paths generated between progressively divergent protein pairs, some of which do not even acquire the same structural fold. The ease of interpolating between two sequences could be used as a proxy for the likelihood of homology between them.

Sustaining 500,000 Folding Cycles Through Bioinspired Stress Dispersion Design in Sodium‐Ion Batteries

AbstractDeveloping super‐foldable electronic materials and devices presents a significant challenge, as intrinsic conductive materials are unable to achieve numerous true‐folding operations (super‐foldable) due to limitations from short‐range forces of chemical bonds. Consequently, super‐foldable batteries remain unexplored. This work focused on sodium‐ion batteries as a breakthrough point to advance super‐foldable devices. By employing a “2+1” bioinspired strategy, we stepwise designed and assembled super‐foldable components, from substrates to electrodes, and to ultimately device. This bioinspired approach completely disperses folding stress and thus prevents the breakage of chemical bonds, enabling the successful fabrication of the first super‐foldable ion battery. This battery can withstand true‐folding at any angle, in any direction, and for an unprecedented number of cycles—far outperforming current foldable phones with hinge structures. Remarkably, after 500,000 true‐folding cycles, the battery's microstructure remains intact with no significant degradation of electrochemical performance. Real‐time dynamic folding observations reveal an M‐shaped folding structure within the bioinspired materials, which effectively disperses stress via bulged layers, dispersed arcs, and slidable microgrooves that work together across different directions and dimensions to achieve super‐foldability. Mechanical simulations vividly verify this principle. This work represents a breakthrough in super‐foldable devices, offering valuable insights and promoting practical application for future super‐foldable devices.

Sustaining 500,000 Folding Cycles Through Bioinspired Stress Dispersion Design in Sodium-Ion Batteries.

Developing super-foldable electronic materials and devices presents a significant challenge, as intrinsic conductive materials are unable to achieve numerous true-folding operations (super-foldable) due to limitations from short-range forces of chemical bonds. Consequently, super-foldable batteries remain unexplored. This work focused on sodium-ion batteries as a breakthrough point to advance super-foldable devices. By employing a "2+1" bioinspired strategy, we stepwise designed and assembled super-foldable components, from substrates to electrodes, and to ultimately device. This bioinspired approach completely disperses folding stress and thus prevents the breakage of chemical bonds, enabling the successful fabrication of the first super-foldable ion battery. This battery can withstand true-folding at any angle, in any direction, and for an unprecedented number of cycles-far outperforming current foldable phones with hinge structures. Remarkably, after 500,000 true-folding cycles, the battery's microstructure remains intact with no significant degradation of electrochemical performance. Real-time dynamic folding observations reveal an M-shaped folding structure within the bioinspired materials, which effectively disperses stress via bulged layers, dispersed arcs, and slidable microgrooves that work together across different directions and dimensions to achieve super-foldability. Mechanical simulations vividly verify this principle. This work represents a breakthrough in super-foldable devices, offering valuable insights and promoting practical application for future super-foldable devices.

Differentiation and quantification of bovine and pork gelatin using UPLC-QTOF and ATR-FTIR spectroscopy: Addressing challenges in mixed gelatin analysis and detection

The amino acid sequence dictates protein folding and spatial structure, essential for understanding their behavior. Gelatin, important in industry and biomedicine, demands accurate source authentication due to ethical and dietary concerns. This study explores differentiating and quantifying bovine and pork gelatin using UPLC-QTOF and ATR-FTIR spectroscopy. UPLC-QTOF identified distinct ions for pure bovine (m/z + 962.1471, NRLHFFK) and pork gelatin (m/z + 653.0289, YNEVK) but struggled with mixed gelatins due to protein-protein interactions altering peptide ion profiles. ATR-FTIR was employed to leverage ethanol's differential effects on gelatin's amide bands for quantifying pork gelatin contamination in bovine gelatin. The method showed a strong linear correlation (R2 = 0.9994) with contamination levels and amide band transmission, with detection and quantification limits of 0.85 and 2.85 mg/100 mg, respectively. It effectively identified pork gelatin in halal candy, with recovery rates from 50.05 % to 103.69 %, highlighting ATR-FTIR's potential for accurate gelatin analysis.

3D chromatin maps of a brown alga reveal U/V sex chromosome spatial organization.

Nuclear three dimensional (3D) folding of chromatin structure has been linked to gene expression regulation and correct developmental programs, but little is known about the 3D architecture of sex chromosomes within the nucleus, and how that impacts their role in sex determination. Here, we determine the sex-specific 3D organization of the model brown alga Ectocarpus chromosomes at 2 kb resolution, by mapping long-range chromosomal interactions using Hi-C coupled with Oxford Nanopore long reads. We report that Ectocarpus interphase chromatin exhibits a non-Rabl conformation, with strong contacts among telomeres and among centromeres, which feature centromere-specific LTR retrotransposons. The Ectocarpus chromosomes do not contain large local interactive domains that resemble TADs described in animals, but their 3D genome organization is largely shaped by post-translational modifications of histone proteins. We show that the sex determining region (SDR)within the U and V chromosomes are insulated and span the centromeres andwe link sex-specific chromatin dynamics and gene expression levels to the 3D chromatin structure of the U and V chromosomes. Finally, we uncover the unique conformation of a large genomic region on chromosome 6 harboring an endogenous viral element, providing insights regarding the impact of a latent giant dsDNA virus on the host genome's 3D chromosomal folding.

Teleseismic virtual-source reverse time migration of upper crustal structures in the Three Gorges region, China

SUMMARY The Three Gorges (TG) in central China is an earthquake prone region that lacks active-source seismic surveys, hence requiring high-resolution passive seismic imaging to reveal crustal structures in detail. While teleseismic virtual-source reflection (TVR) profiling is effective for imaging gently dipping upper crustal structures, it is unsuitable for mapping steep structures beneath rugged topography in the TG region. Here we develop a teleseismic virtual-source reverse time migration (TV-RTM) to improve the imaging of steep structures. Synthetic tests are conducted to demonstrate the validity and resolution of the TV-RTM method. To mitigate the imaging inaccuracy due to sparse station spacing, we interpolate direct-arrival waveforms to achieve a doubling of the minimally required station spacing from 2 to 4 km. The TV-RTM images of the upper crustal structure beneath a 2-D array in the TG region reveal significant fold and thrust structures that correlate well with the surface geology and tectonic framework. The resolution of the images is assessed using 2-D and 3-D synthetic models with the station and source geometry of field data. The TV-RTM method provides a new passive seismic solution for studying upper crustal structures in regions that lack active-source seismic data.

Molecular Lineages and Spatial Distributions of Subplate Neurons in the Human Fetal Cerebral Cortex.

The expansion of neural progenitors and production of distinct neurons are crucial for architectural assembly and formation of connectivity in human brains. Subplate neurons (SPNs) are among the firstborn neurons in the human fetal cerebral cortex, and play a critical role in establishing intra- and extracortical connections. However, little is known about SPN origin and developmental lineages. In this study, spatial landscapes and molecular trajectories of SPNs in the human fetal cortices from gestational weeks (GW) 10 to 25 are created by performing spatial transcriptomics and single-cell RNA sequencing. Genes known to be evolutionarily human-specific and genes associated with extracellular matrices (ECMs) are found to maintain stable proportions of subplate neurons among other neuronal types. Enriched ECM gene expression in SPNs varies in distinct cortical regions, with the highest level in the frontal lobe of human fetal brains. This study reveals molecular origin and lineage specification of subplate neurons in the human fetal cerebral cortices, and highlights underpinnings of SPNs to cortical neurogenesis and early structural folding.