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Creators/Authors contains: "Hasegawa, Takeshi"

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  1. 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 
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  2. Abstract. Volcanic fallout in polar ice sheets provides important opportunities to date and correlate ice-core records as well as to investigate theenvironmental impacts of eruptions. Only the geochemical characterization of volcanic ash (tephra) embedded in the ice strata can confirm the sourceof the eruption, however, and is a requisite if historical eruption ages are to be used as valid chronological checks on annual ice layercounting. Here we report the investigation of ash particles in a Greenland ice core that are associated with a volcanic sulfuric acid layer previouslyattributed to the 79 CE eruption of Vesuvius. Major and trace element composition of the particles indicates that the tephra does not derive fromVesuvius but most likely originates from an unidentified eruption in the Aleutian arc. Using ash dispersal modeling, we find that only an eruptionlarge enough to include stratospheric injection is likely to account for the sizable (24–85 µm) ash particles observed in the Greenlandice at this time. Despite its likely explosivity, this event does not appear to have triggered significant climate perturbations, unlike some otherlarge extratropical eruptions. In light of a recent re-evaluation of the Greenland ice-core chronologies, our findings further challenge the previousassignation of this volcanic event to 79 CE. We highlight the need for the revised Common Era ice-core chronology to be formally accepted by the widerice-core and climate modeling communities in order to ensure robust age linkages to precisely dated historical and paleoclimate proxy records. 
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