Two-dimensional NMR lineshape analysis

NMR titration experiments are a rich source of structural, mechanistic, thermodynamic and kinetic information on biomolecular interactions, which can be extracted through the quantitative analysis of resonance lineshapes. However, applications of such analyses are frequently limited by peak overlap inherent to complex biomolecular systems. Moreover, systematic errors may arise due to the analysis of two-dimensional data using theoretical frameworks developed for one-dimensional experiments. Here we introduce a more accurate and convenient method for the analysis of such data, based on the direct quantum mechanical simulation and fitting of entire two-dimensional experiments, which we implement in a new software tool, TITAN (TITration ANalysis). We expect the approach, which we demonstrate for a variety of protein-protein and protein-ligand interactions, to be particularly useful in providing information on multi-step or multi-component interactions

Intramolecular Cohesion of Coils Mediated by Phenylalanine–Glycine Motifs in the Natively Unfolded Domain of a Nucleoporin

The nuclear pore complex (NPC) provides the sole aqueous conduit for macromolecular exchange between the nucleus and the cytoplasm of cells. Its diffusion conduit contains a size-selective gate formed by a family of NPC proteins that feature large, natively unfolded domains with phenylalanine–glycine repeats (FG domains). These domains of nucleoporins play key roles in establishing the NPC permeability barrier, but little is known about their dynamic structure. Here we used molecular modeling and biophysical techniques to characterize the dynamic ensemble of structures of a representative FG domain from the yeast nucleoporin Nup116. The results showed that its FG motifs function as intramolecular cohesion elements that impart order to the FG domain and compact its ensemble of structures into native premolten globular configurations. At the NPC, the FG motifs of nucleoporins may exert this cohesive effect intermolecularly as well as intramolecularly to form a malleable yet cohesive quaternary structure composed of highly flexible polypeptide chains. Dynamic shifts in the equilibrium or competition between intra- and intermolecular FG motif interactions could facilitate the rapid and reversible structural transitions at the NPC conduit needed to accommodate passing karyopherin–cargo complexes of various shapes and sizes while simultaneously maintaining a size-selective gate against protein diffusion

Room-temperature entanglement between single defect spins in diamond

Entanglement is the central yet fleeting phenomenon of quantum physics. Once being considered a peculiar counter-intuitive property of quantum theory1, it has developed into the most central element of quantum technology. Consequently, there have been a number of experimental demonstrations of entanglement between photons2, atoms3, ions4 and solid-state systems such as spins or quantum dots5, 6, 7, superconducting circuits8, 9 and macroscopic diamond10. Here we experimentally demonstrate entanglement between two engineered single solid-state spin quantum bits (qubits) at ambient conditions. Photon emission of defect pairs reveals ground-state spin correlation. Entanglement (fidelity = 0.67±0.04) is proved by quantum state tomography. Moreover, the lifetime of electron spin entanglement is extended to milliseconds by entanglement swapping to nuclear spins. The experiments mark an important step towards a scalable room-temperature quantum device being of potential use in quantum information processing as well as metrology