Radio-frequency association of molecules: an assisted Feshbach resonance

We develop a theoretical model to describe the radio-frequency (rf) induced coupling of a pair of colliding atoms to a Feshbach molecule when a magnetic field arbitrarily far from the Feshbach resonance is modulated in time. We use the dressed atom picture, and show that the coupling strength in presence of rf is equal to the Feshbach coupling strength multiplied by the square of a Bessel function. The argument of this function is equal to the ratio of the atomic rf Rabi frequency to the rf frequency. We experimentally demonstrate this law by measuring the rate of rf-association of molecules using a Feshbach resonance in d wave collisions between ultra-cold chromium atoms.     

Electronic influence of water adsorbed on ZnO in H2 and Co oxidation

In this paper we calculate the effect of surface OH/OH^– on the simultaneous adsorption of H₂ and O₂ on ZnO. A quantitative comparison between H₂ and CO oxidation rates shows that the two mechanisms are similar for the same water recovery on ZnO.

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OH/OH^– H₂ O₂ ZnO. H₂ CO , ZnO.

     

Chemical Development of Intracellular Protein Heterodimerizers

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Highlights? Design of cell-permeable, SNAP-tag and HaloTag reactive, covalent dimerizers (HaXS) ? HaXS dimerizers force rapid intracellular dimerization of tagged proteins of interest ? In contrast to rapalogs, HaXS8 does not interfere with PI3K/mTOR signaling ? HaXS8 is compatible with multiplexed approaches using other CIDs     

Cell‐Permeant and Photocleavable Chemical Inducer of Dimerization

Chemical inducers of dimerization (CIDs) have been developed to orchestrate protein dimerization and translocation. Here we present a novel photocleavable HaloTag‐ and SNAP‐tag‐reactive CID (MeNV‐HaXS) with excellent selectivity and intracellular reactivity. Excitation at 360 nm cleaves the methyl‐6‐nitroveratryl core of MeNV‐HaXS. MeNV‐HaXS covalently links HaloTag‐ and SNAP‐tag fusion proteins, and enables targeting of selected membranes and intracellular organelles. MeNV‐HaXS‐mediated translocation has been validated for plasma membrane, late endosomes, lysosomes, Golgi, mitochondria, and the actin cytoskeleton. Photocleavage of MeNV‐HaXS liberates target proteins and provides access to optical manipulation of protein relocation with high spatiotemporal and subcellular precision. MeNV‐HaXS supports kinetic studies of protein dynamics and the manipulation of subcellular enzyme activities, which is exemplified for Golgi‐targeted cargo and the assessment of nuclear import kinetics.     

Interfacial properties of heat-treated ovalbumin

The interfacial properties (kinetics of adsorption at the air/water interface, rheology of the interfacial layer) of ovalbumin molecules, unheated or previously heat-denatured in solution (10 g L(-1), pH 7, NaCl 50 mM) under controlled conditions (up to 40 min at 80 degrees C), were investigated. Heat treatments induced the formation of covalent aggregates which surface exhibits a higher hydrophobicity and an increased exposition of sulfhydryl groups when compared to native ovalbumin (unheated). Although they have a larger hydrodynamic size, aggregates adsorb as fast as native ovalbumin at the air/water interface. However, aggregates are able to established rapid contacts in the interfacial layer as shown by the fast increase of both surface pressure and shear elastic constant. In contrast, native ovalbumin needs longer time to developed intermolecular contacts and exhibits lower foam stability even if the shear elastic constant on aging reached higher value than for ovalbumin aggregates.