Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process

: Small Heat Shock Proteins (sHSPs) are key components of our Protein Quality Control system and are thought to act as reservoirs that neutralize irreversible protein aggregation. Yet, sHSPs can also act as sequestrases, promoting protein sequestration into aggregates, thus challenging our understanding of their exact mechanisms of action. Here, we employ optical tweezers to explore the mechanisms of action of the human small heat shock protein HSPB8 and its pathogenic mutant K141E, which is associated with neuromuscular disease. Through single-molecule manipulation experiments, we studied how HSPB8 and its K141E mutant affect the refolding and aggregation processes of the maltose binding protein. Our data show that HSPB8 selectively suppresses protein aggregation without affecting the native folding process. This anti-aggregation mechanism is distinct from previous models that rely on the stabilization of unfolded polypeptide chains or partially folded structures, as has been reported for other chaperones. Rather, it appears that HSPB8 selectively recognizes and binds to aggregated species formed at the early stages of aggregation, preventing them from growing into larger aggregated structures. Consistently, the K141E mutation specifically targets the affinity for aggregated structures without impacting native folding, and hence impairs its anti-aggregation activity

Synthesis and characterization of atomically-thin graphite films on a silicon carbide substrate

This paper reports the synthesis and detailed characterization of graphite thin films produced by thermal decomposition of the (0001) face of a 6H-SiC wafer, demonstrating the successful growth of single crystalline films down to approximately one graphene layer. The growth and characterization were carried out in ultrahigh vacuum (UHV) conditions. The growth process and sample quality were monitored by low-energy electron diffraction, and the thickness of the sample was determined by core level x-ray photoelectron spectroscopy. High-resolution angle-resolved photoemission spectroscopy shows constant energy map patterns, which are very sharp and fully momentum-resolved, but nonetheless not resolution limited. We discuss the implications of this observation in connection with scanning electron microscopy data, as well as with previous studies

Pathways towards Legal Migration into the EU: Reappraising concepts, trajectories and policies. CEPS Paperback, September 2017

On 27 January 2017, the Justice and Home Affairs Section of CEPS and the Directorate-General for Migration and Home Affairs (DG HOME) of the European Commission co-organised a policy workshop in Brussels entitled “Reappraising the EU legal migration acquis: Legal pathways for a new model of economic migration, and the role of social science research”. The event brought together leading academics, practitioners and European Commission representatives to assess and discuss the state of play in the (internal and external) EU legal migration acquis, and its role in developing legal pathways towards economic migration. Held under the Chatham House Rule, the policy workshop’s roundtable discussions allowed participants to identify and address some of the key challenges, inconsistencies and gaps in the standing EU policies and legislation in the area of legal and economic migration. Scholars involved in EU and nationally funded, collaborative research projects on social science and humanities (SSH) had the opportunity to exchange interdisciplinary knowledge with European Commission officials representing the different services working on legal migration policies. The role and potential of independent academic research in the framework of EU migration policymaking were also discussed. The full programme of the policy workshop is reproduced in the annex of this book

Global estimates of biomass burning emissions based on satellite imagery for the year 2000

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/94645/1/jgrd11177.pd