Quantum interference in atom-exchange reactions.

Chemical reactions, in which bonds break and form, are highly dynamic quantum processes. A fundamental question is whether coherence can be preserved in chemical reactions and then harnessed to generate entangled products. Here we investigated this question by studying the 2KRb [Formula: see text][Formula: see text] + Rb reaction at 500 nanokelvins, focusing on the nuclear spin degrees of freedom.

Measurement of the Excitation Spectrum of a Dipolar Gas in the Macrodroplet Regime.

The excitation spectrum of a cigar-shaped strongly dipolar quantum gas at the crossover from a Bose-Einstein condensate to a trapped macrodroplet is predicted to exhibit peculiar features-a strong upward shift of low momentum excitation energies together with a strong multiband response for high momenta. By performing Bragg spectroscopy over a wide range of momenta, we observe both key elements and also confirm the predicted stiffening of excitation modes when approaching the macrodroplet regime. Our measurements are in good agreement with numerical calculations taking into account finite size effects.

Efficient synthesis of enantiopure amines from alcohols using resting cells and ammonia.

-Chiral amines are pivotal building blocks for chemical manufacturing. Stereoselective amination of alcohols is receiving increased interest due to its higher atom-efficiency and overall improved environmental footprint compared with other chemocatalytic and biocatalytic methods. We previously developed a hydrogen-borrowing amination by combining an alcohol dehydrogenase (ADH) with an amine dehydrogenase (AmDH) .

Lysosomes nor Mice Move Forward without Borcs7.

Lysosome function and position in the cytoplasm depends on the BORCS machinery, which tethers lysosomes to the kinesin microtubule motor. A recent paper of Snouwaert et al. in Cell Reports characterizes a mouse with a spontaneous mutation in the Borcs7 subunit, which causes axonal dystrophy and impaired motor function.

Concurrent presence of on- and off-pathway folding intermediates of apoflavodoxin at physiological ionic strength.

Flavodoxins have a protein topology that can be traced back to the universal ancestor of the three kingdoms of life. Proteins with this type of architecture tend to temporarily misfold during unassisted folding to their native state and form intermediates. Several of these intermediate species are molten globules (MGs), which are characterized by a substantial amount of secondary structure, yet without the tertiary side-chain packing of natively folded proteins.