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The development of computational efficient models is essential to obtain a detailed characterization of the mechanisms underlying the folding of proteins and the formation of amyloid fibrils. Structure-based computational models (Go-model) with Cα or all-atom resolutions have been able to successfully delineate the mechanisms of folding of several globular proteins and offer an interesting alternative to computationally intensive simulations with explicit solvent description. Here, we explore the limits of Go-model predictions by analyzing the folding of the nonglobular repeat domain proteins Notch Ankyrin and p16INK4and the formation of human islet amyloid polypeptide (hIAPP) fibrils. Folding trajectories of the repeat domain proteins revealed that an all-atom resolution is required to capture the folding pathways and cooperativity reported in experimental studies. The all-atom Go-model was also successful in predicting the free-energy landscape of hIAPP fibrillation, suggesting a “dock and lock” mechanism of fibril elongation. We finally explored how mutations can affect the co-assembly of hIAPP fibrils by simulating a heterogeneous system composed of wild-type and mutated hIAPP peptides. Overall, this study shows that all-atom Go-model-based simulations have the potential of discerning the effects of mutations and post-translational modifications in protein folding and association and may help in resolving the dichotomy between experimental and theoretical studies on protein folding and amyloid fibrillation.

Disrupted-in-schizophrenia-1 (DISC1) is a scaffold protein of significant importance for neuro-development and a prominent candidate protein in the etiology of mental disorders. In this work, we investigate the role of conformational heterogeneity and local structural disorder in the oligomerization pathway of the full-length DISC1and of two truncation variants. Through extensive coarse-grained molecular dynamics simulations with a predictive energy landscape-based model, we shed light on the interplay of local and global disorder which lead to different oligomerization pathways. We found that both global conformational heterogeneity and local structural disorder play an important role in shaping distinct oligomerization trends of DISC1. This study also sheds light on the differences in oligomerization pathways of the full-length protein compared to the truncated variants produced by a chromosomal translocation associated with schizophrenia. We report that oligomerization of full-length DISC1sequence works in a nonadditive manner with respect to truncated fragments that do not mirror the conformational landscape or binding affinities of the full-length unit.

LILLIAD Innovation Learning Centre is a new building that incorporates a refurbishment of the former Central Library of Lille University of Science and Technologies, France, and an extension. LILLIAD is a project that has been developed over ten years and opened in September 2016. Three hubs have been created inside the new building: the library, the research showcase and the events facilities.

Polystyrene (PS) is a major commodity polymer widely used in various applications ranging from packaging to insulation thanks to its low cost, high stiffness, and transparency as well as its relatively high softening temperature. Similarly to all polymers prepared by radical polymerization, PS is constituted of a C–C backbone and thus is not degradable. To confer degradability to such materials, the copolymerization of vinyl monomers with a cyclic monomer that could undergo radical ring-opening is an efficient method to introduce purposely cleavable bonds into the polymer backbone. Dibenzo[c,e]-oxepane-5-thione (DOT) is a cyclic thionolactone monomer known for its efficient copolymerization with acrylate derivatives but so far could not be incorporated into PS backbones. From a theoretical study combining density functional theory (DFT) and kinetic models using the PREDICI software, we showed that the modification of experimental conditions could overcome these limitations and that high molar mass degradable polystyrene (Mwclose to 150 000 g·mol–1) could be prepared via statistical insertion of thioester groups into the polymer backbone. This copolymerization process is compatible with conventional free radical polymerization and reversible deactivation radical polymerization (RDRP) techniques such as nitroxide mediated polymerization (NMP). Thanks to favorable reactivity ratios allowing only a few mol % of thioester units to be randomly incorporated, there was no major modification of the thermal and mechanical properties of the PS. The degradation of such PS could be performed in tetrahydrofuran (THF) at room temperature (RT) in 1 h using 1,5,7-triazabicyclo[4.4.0]dec-5-ene (TBD) as a base, leading to oligomers with Mnclose to 2000 g·mol–1. We successfully demonstrate further applicability of these copolymerization systems for the phototriggered decomposition of PS in solution as well as the synthesis of cross-linked PS networks degradable into soluble side products.

A research disclosure about the Ethocel Ethylcellulose chemistry manufactured by Dow Chemical Co. is presented. It is a film-forming cellulosic polymer with the ability to structure various oil bases and solvents. Despite its limited compatibility in pure oils and solvents, the product can be a useful formulation tool.

Although it is now relatively well understood how sequence defines and impacts global protein stability in specific structural contexts, the question of how sequence modulates the configurational landscape of proteins remains to be defined. Protein configurational equilibria are generally characterized by using various chemical denaturants or by changing temperature or pH. Another thermodynamic parameter which is less often used in such studies is high hydrostatic pressure. This review discusses the basis for pressure effects on protein structure and stability, and describes how the unique mechanisms of pressure-induced unfolding can provide unique insights into protein conformational landscapes.

The article previews the 2013-2014 leadership seminar organized by the Ligue européenne des bibliothèques de recherche (Liber), or European league of research libraries. Information is also given about the league's establishment of the seminar during the mid-2000s.