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Key Points Provenance changes at the outlet of the Hetao Basin indicate the desiccation and re‐integration of the upper Yellow River over the last ∼40 ka Paleo‐lake shorelines and geochemical proxies confirm that the west Hetao Basin contained the terminal lake for the desiccated Yellow River Climate‐river feedbacks across glacial‐interglacial cycles have implications for constraining terrestrial‐marine source‐to‐sink processes 

Abstract Protein’s magic function stems from its structure and various analytical techniques have been developed for it. Among proteins, membrane proteins are encoded 20–30% of genomes, whereas cause challenges for many analytical techniques. For example, lots of membrane proteins cannot form single crystal structure required by X-ray crystallography. As for NMR, the measurements were hindered by the low tumbling rates of membrane (i.e., phospholipid bilayers) where membrane proteins exist. In addition, membrane proteins usually lay parallel to the surface of phospholipid bilayers or form transmembrane structure. No matter parallel or perpendicular to phospholipid bilayers surface, membrane proteins form monolayer structure which is also difficult for X-ray and NMR to provide high-resolution results. Because NMR and X-ray crystallography are the two major analytical techniques to address protein’s structure, membrane proteins only contribute 2.4% to the solved protein databank. Surface FT-IR techniques can evaluate the conformation and orientation of membrane proteins by amide I band. Specifically for α-helical peptides/proteins, the orientation of the axis is critical to decide whether proteins form transmembrane structure. Notice that the traditional FT-IR can only provide “low-resolution” results.Here,¹³C isotope was introduced into the nonamyloid component (NAC), which spans residues 61–95 of α-synuclein (α-syn). Then, p-polarized multiple-angle incidence resolution spectrometry (pMAIRS) was used to determine the orientation of a specific residue of α-helical NAC in monolayer. In general, pMAIRS is a novel technique to work complementary with X-ray and NMR to address membrane peptides/proteins structure with high resolution even in monolayer. Graphical abstract 

Abstract Current barriers hindering data-driven discoveries in deep-time Earth (DE) include: substantial volumes of DE data are not digitized; many DE databases do not adhere to FAIR (findable, accessible, interoperable and reusable) principles; we lack a systematic knowledge graph for DE; existing DE databases are geographically heterogeneous; a significant fraction of DE data is not in open-access formats; tailored tools are needed. These challenges motivate the Deep-Time Digital Earth (DDE) program initiated by the International Union of Geological Sciences and developed in cooperation with national geological surveys, professional associations, academic institutions and scientists around the world. DDE’s mission is to build on previous research to develop a systematic DE knowledge graph, a FAIR data infrastructure that links existing databases and makes dark data visible, and tailored tools for DE data, which are universally accessible. DDE aims to harmonize DE data, share global geoscience knowledge and facilitate data-driven discovery in the understanding of Earth's evolution.