'Initiators of Discursive Practices': Authorship, attribution, and intent in the debates between philosophes and anti-philosophes

This article focuses on the “social side” of pseudonymity—on how writers and readers compete to influence the critical destiny of a pseudonymous work. By analyzing pseudonymity and attribution in both the specific context of Voltaire’s 1760 staging of the play, Le café ou l’écossaise, and in larger debates in the emerging fields of anonymity, pseudonymity, and attribution studies, I hope to show how literary scholars at present can address the individuality of each pseudonymous case while not letting go of trans-historical, general problems of anonymous strategies. Voltaire’s use of multiple pseudonyms before and after releasing L’Ecossaise, a comédie sérieuse in which Voltaire attacks his enemy Elie-Cathérine Fréron, supports his philosophe friends at a crucial moment in history, and exemplifies his emerging taste for serious comedy and British drama calls into question traditional takes on pseudonymity, anonymity, and attribution by refusing to fit into the binary arguments of anonymous vs. attributed and authorial intent vs. the reader’s control.

Structural Analysis of alpha-Fetoprotein (AFP)-like Peptides with Anti-Breast-Cancer Properties

The abundance of alpha-fetoprotein (AFP), a natural protein produced by the fetal yolk sac during pregnancy, correlates with lower incidence of estrogen receptor positive (ER+) breast cancer. The pharmacophore region of AFP has been narrowed down to a four amino acid (AA) region in the third domain of the 591 AA peptide. Our computational study focuses on a 4-mer segment consisting of the amino acids threonine-proline-valine-asparagine (TPVN). We have run replica exchange molecular dynamics (REMD) simulations and used 120 configurational snapshots from the total trajectory as starting configurations for quantum chemical calculations. We optimized structures using semiempirical (PM3, PM6, PM6-D2, PM6-H2, PM6-DH+, PM6-DH2) and density functional methods (TPSS, PBE0, M06-2X). By comparing the accuracy of these methods against RI-MP2 benchmarks, we devised a protocol for calculating the lowest energy conformers of these peptides accurately and efficiently. This protocol screens out high-energy conformers using lower levels of theory and outlines a general method for predicting small peptide structures.