"Illusory" illusory conjunctions: The conjoining of features of visual and imagined stimuli.

The question of whether illusory conjunctions would occur with visual mental imagery was investigated. In 4 experiments, participants were tachistoscopically presented displays of geometrical figures (varying in shape, color, and solidity) flanked by 2 digits. For half of the trials, participants imagined one of the figures in the display. Illusory conjunctions occurred between the features of the physical (cued) and imagined figures, which suggests that imagery influences perception at the level of visual processing at which features are combined. Moreover, the conjunction errors induced by an imagined figure were similar to those induced by a physical figure with the same features. The pattern of errors could not be accounted for by guessing. Together, these findings support the view that there can be correspondence between visual imagery and visual perception. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Tim9, a new component of the TIM22.54 translocase in mitochondria

We have identified Tim9, a new component of the TIM22.54 import machinery, which mediates transport of proteins into the inner membrane of mitochondria. Tim9, an essential protein of Saccharomyces cerevisiae, shares sequence similarity with Tim10 and Tim12. Tim9 is located in the mitochondrial intermembrane space and is organized into two distinct hetero-oligomeric assemblies with Tim10 and Tim12. One complex contains Tim9 and Tim10. The other complex contains Tim9, Tim10 and Tim12 and is tightly associated with Tim22 in the inner membrane. The TIM9.10 complex is more abundant than the TIM9.10.12 complex and mediates partial translocation of mitochondrial carriers proteins across the outer membrane. The TIM9.10.12 complex assists further translocation into the inner membrane in association with TIM22.54.     

分离乙醇的过程

正本发明涉及到操作蒸馏塔分离乙醇混合物的过程,乙醇混合物含有乙醇和醋酸,该过程回收的乙醇含醋酸量小于700wppm。蒸馏塔的操作条件可以根据加料组分变化。具体说,过程提供了具有低醋酸浓     

Phase-changing sacrificial materials for interfacing microfluidics with ion-permeable membranes to create on-chip preconcentrators and electric field gradient focusing microchips

We have developed a novel approach for interfacing ionically conductive membranes with microfluidic systems using phase-changing sacrificial layers. Imprinted microchannels in a polymer substrate are filled with a heated liquid that solidifies at room temperature, a monomer solution is placed over the protected channels and polymerized to form a rigid semipermeable copolymer, and then the protective layer is melted and removed, leaving an open microchannel interfaced with a polymer membrane. We have applied this method in miniaturizing electric field gradient focusing (EFGF) and carrying out on-chip protein preconcentration. A semipermeable copolymer in the EFGF microchips fills a region of changing cross-sectional area, which allows a gradient in electric field to be established when an electrical potential is applied. Our technique provides microchip EFGF devices that offer 3-fold improved resolution in protein focusing compared with capillary-based systems. In addition, these EFGF microchips can separate peptide samples with resolution similar to what is obtained in capillary electrophoresis microdevices, and the micro-EFGF systems enrich analytes by a factor of >150. Finally, we have fabricated membrane-integrated microfluidic devices that can concentrate protein samples (R-phycoerythrin) over 10 000-fold to facilitate microchip capillary electrophoresis. Interfacing microchannels with ion-permeable membranes has great potential to enhance microchip analysis of biomolecules.     

Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase

Isopenicillin N synthase (IPNS) is a non-heme iron(ii)-dependent oxidase that is central to penicillin biosynthesis. Herein, we report mechanistic studies of the IPNS reaction in the crystalline state, using the substrate analogue delta-(L-alpha-aminoadipoyl)-(3R)-methyl-L-cysteine D-alpha-hydroxyisovaleryl ester (AmCOV) to probe the early stages of the catalytic cycle. The X-ray crystal structure of the anaerobic IPNS:Fe(II):AmCOV complex was solved to 1.40 A resolution, and it reveals several subtle differences in the active site relative to the complex of the enzyme with its natural substrate. The crystalline IPNS:Fe(II):AmCOV complex was then exposed to oxygen gas at high pressure; this brought about reaction to give what appears to be a hydroxymethyl/ene-thiol product. A mechanism for this reaction is proposed. These results offer further insight into the delicate interplay of steric and electronic effects in the IPNS active site and the mechanistic intricacies of this remarkable enzyme.