Métaphysique et Rationalisme. Le débat littéraire aux Pays-Bas entre 1916 et 1950

Le débat littéraire aux Pays-Bas, contrairement à ce qui fut le cas en Flandre, s’est tenu à l’écart de la vie intellectuelle du reste de l’Europe. L’opposition entre « l’art pour l’art » et l’engagement a joué un rôle plus profond, de pair avec le conflit traditionnel entre catholicisme et protestantisme, romantisme et rationalisme, métaphysique et réalisme. Les personnages principaux de ce débat : Slauerhoff, Théo van Doesburg mais surtout Nijhoff, Marsman, Ter Braak et enfin Cola Debrot qui fut la synthèse des deux pôles (Nijhoff et Ter Braak).De Nederlandse literaire discussie heeft zieh, in tegenstelling tot de Vlaamse, afzijdig gehouden van de rest van Europa. Het contrast tussen « l’art pour l’art » en maatschappelijk engagement heeft in het Noorden een längere doorwerking gehad, dit samen met de traditionele strijd tussen katholicisme en protestantisme, romantisme en rationalisme, metafysiek en realisme. De hoofdpersonnages van dit debat: Slauerhoff, Theo van Doesburg maar vooral Martinus Nijhoff, Marsman, Ter Braak en uiteindelijk Cola Debrot dit de twee belangrijkste polen, Nijhoff en Ter Braak, in zieh verenigde

Characterizing stable complete Erdös space

We focus on the space

Effects of Macromolecular Crowding on Protein Conformational Changes

Many protein functions can be directly linked to conformational changes. Inside cells, the equilibria and transition rates between different conformations may be affected by macromolecular crowding. We have recently developed a new approach for modeling crowding effects, which enables an atomistic representation of “test” proteins. Here this approach is applied to study how crowding affects the equilibria and transition rates between open and closed conformations of seven proteins: yeast protein disulfide isomerase (yPDI), adenylate kinase (AdK), orotidine phosphate decarboxylase (ODCase), Trp repressor (TrpR), hemoglobin, DNA β-glucosyltransferase, and Ap4A hydrolase. For each protein, molecular dynamics simulations of the open and closed states are separately run. Representative open and closed conformations are then used to calculate the crowding-induced changes in chemical potential for the two states. The difference in chemical-potential change between the two states finally predicts the effects of crowding on the population ratio of the two states. Crowding is found to reduce the open population to various extents. In the presence of crowders with a 15 Å radius and occupying 35% of volume, the open-to-closed population ratios of yPDI, AdK, ODCase and TrpR are reduced by 79%, 78%, 62% and 55%, respectively. The reductions for the remaining three proteins are 20–44%. As expected, the four proteins experiencing the stronger crowding effects are those with larger conformational changes between open and closed states (e.g., as measured by the change in radius of gyration). Larger proteins also tend to experience stronger crowding effects than smaller ones [e.g., comparing yPDI (480 residues) and TrpR (98 residues)]. The potentials of mean force along the open-closed reaction coordinate of apo and ligand-bound ODCase are altered by crowding, suggesting that transition rates are also affected. These quantitative results and qualitative trends will serve as valuable guides for expected crowding effects on protein conformation changes inside cells