Imbalance of Hsp70 family variants fosters tau accumulation

Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/154405/1/fsb2027004018.pd

Entanglement in helium

Using a configuration-interaction variational method, we accurately compute the reduced, single-electron von Neumann entropy for several low-energy, singlet and triplet eigenstates of helium atom. We estimate the amount of electron-electron orbital entanglement for such eigenstates and show that it decays with energy.Comment: 5 pages, 2 figures, added references and discussio

The simplest double slit: Interference and entanglement in double photoionization of H2

The wave nature of particles is rarely observed, in part because of their very short de Broglie wavelengths in most situations. However, even with wavelengths close to the size of their surroundings, the particles couple to their environment (for example, by gravity, Coulomb interaction, or thermal radiation). These couplings shift the wave phases, often in an uncontrolled way, and the resulting decoherence, or loss of phase integrity, is thought to be a main cause of the transition from quantum to classical behavior. How much interaction is needed to induce this transition? Here we show that a photoelectron and two protons form a minimum particle/slit system and that a single additional electron constitutes a minimum environment. Interference fringes observed in the angular distribution of a single electron are lost through its Coulomb interaction with a second electron, though the correlated momenta of the entangled electron pair continue to exhibit quantum interference.This work was supported by the Deutsche Forschungsgemeinschaft and by the Office of Basic Energy Sciences, Division of Chemical Sciences of the U. S. Department of Energy under contract DE-AC03-76SF00098.Peer Reviewe

Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer

International audienceMisfolding of the microtubule-associated protein Tau is a hallmark of Alzheimer disease and several other neurodegenerative disorders. Because of the dynamic nature of the Tau protein, little is known however about the changes in Tau structure that occur during misfolding. Here we studied the structural consequences upon binding of the repeat domain of Tau, which plays a key role in pathogenic aggregation, to an aggregation enhancer. By combining NMR experiments with molecular simulations we show that binding of the aggregation enhancer polyglutamic acid remodels the conformational ensemble of Tau. Our study thus provides insight into an early event during misfolding of Tau. This article is protected by copyright. All rights reserved