Search results for: So Iwata
Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 2

Search results for: So Iwata

2 Hydraulic Analysis on Microhabitat of Benthic Macroinvertebrates at Riparian Riffles

Authors: Jin-Hong Kim

Abstract:

Hydraulic analysis on microhabitat of Benthic Macro- invertebrates was performed at riparian riffles of Hongcheon River and Gapyeong Stream. As for the representative species, Ecdyonurus kibunensis, Paraleptophlebia cocorata, Chironomidae sp. and Psilotreta kisoensis iwata were chosen. They showed hydraulically different habitat types by flow velocity and particle diameters of streambed materials. Habitat conditions of the swimmers were determined mainly by the flow velocity rather than by flow depth or by riverbed materials. Burrowers prefer sand and silt, and inhabited at the riverbed. Sprawlers prefer cobble or boulder and inhabited for velocity of 0.05-0.15 m/s. Clingers prefer pebble or cobble and inhabited for velocity of 0.06-0.15 m/s. They were found to be determined mainly by the flow velocity.

Keywords: benthic macroinvertebrates, riffles, clinger, swimmer, burrower, sprawler

Procedia PDF Downloads 167
1 Excited State Structural Dynamics of Retinal Isomerization Revealed by a Femtosecond X-Ray Laser

Authors: Przemyslaw Nogly, Tobias Weinert, Daniel James, Sergio Carbajo, Dmitry Ozerov, Antonia Furrer, Dardan Gashi, Veniamin Borin, Petr Skopintsev, Kathrin Jaeger, Karol Nass, Petra Bath, Robert Bosman, Jason Koglin, Matthew Seaberg, Thomas Lane, Demet Kekilli, Steffen Brünle, Tomoyuki Tanaka, Wenting Wu, Christopher Milne, Thomas A. White, Anton Barty, Uwe Weierstall, Valerie Panneels, Eriko Nango, So Iwata, Mark Hunter, Igor Schapiro, Gebhard Schertler, Richard Neutze, Jörg Standfuss

Abstract:

Ultrafast isomerization of retinal is the primary step in a range of photoresponsive biological functions including vision in humans and ion-transport across bacterial membranes. We studied the sub-picosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin using an X-ray laser. Twenty snapshots with near-atomic spatial and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket prior to passing through a highly-twisted geometry and emerging in the 13-cis conformation. The aspartic acid residues and functional water molecules in proximity of the retinal Schiff base respond collectively to formation and decay of the initial excited state and retinal isomerization. These observations reveal how the protein scaffold guides this remarkably efficient photochemical reaction.

Keywords: bacteriorhodopsin, free-electron laser, retinal isomerization mechanism, time-resolved crystallography

Procedia PDF Downloads 199