The Shadow of Eternity: Belief and Structure in Herbert, Vaughan, and Traherne

The poetry of Herbert, Vaughan, and Traherne represents “an attempt to shape their lives and verse around the fact of divine presence and influence,” writes Sharon Seelig. The relationship between belief and expression in these three metaphysical poets is the subject of this deeply perceptive study. Each of these poets held to some extent the notion of dual reality, of the world as indicative of a higher reality, but their responses to this tradition vary greatly—from the ongoing struggle between God and the poet of The Temple, which finally transforms the materials of everyday life and worship; to the more difficult unity of Silex Scintillans, with its tension between illumination and resignation; to the ecstatic proclamations of Thomas Traherne, whose sense of divine reality at first seems so strong as to destroy the characteristic metaphysical tension between this world and the next. Seelig’s study proceeds from individual poems to the whole work, exploring the relation of cosmology and religious experience to poetic form. Sharon Cadman Seelig has taught English at Smith, Wellesley, and Mount Holyoke Colleges. A graceful, compact study which adds significantly to our appreciation of Herbert, Vaughan, and Traherne. —Seventeenth-Century News An impressive reading of Herbert....Seelig\u27s work resonates with an erudite virtuosity, easily equal to its demanding subject. —Christianity & Literaturehttps://uknowledge.uky.edu/upk_english_language_and_literature_british_isles/1065/thumbnail.jp

Interaction of Tau Protein with Model Lipid Membranes Induces Tau Structural Compaction and Membrane Disruption

The misfolding and aggregation of the intrinsically disordered, microtubule-associated tau protein into neurofibrillary tangles is implicated in the pathogenesis of Alzheimer's disease. However, the mechanisms of tau aggregation and toxicity remain unknown. Recent work has shown that anionic lipid membranes can induce tau aggregation and that membrane permeabilization may serve as a pathway by which protein aggregates exert toxicity, suggesting that the plasma membrane may play dual roles in tau pathology. This prompted our investigation to assess tau's propensity to interact with membranes and to elucidate the mutually disruptive structural perturbations the interactions induce in both tau and the membrane. We show that although highly charged and soluble, the full-length tau (hTau40) is also highly surface active, selectively inserts into anionic DMPG lipid monolayers and induces membrane morphological changes. To resolve molecular-scale structural details of hTau40 associated with lipid membranes, X-ray and neutron scattering techniques are utilized. X-ray reflectivity indicates hTau40s presence underneath a DMPG monolayer and penetration into the lipid headgroups and tailgroups, whereas grazing incidence X-ray diffraction shows that hTau40 insertion disrupts lipid packing. Moreover, both air/water and DMPG lipid membrane interfaces induce the disordered hTau40 to partially adopt a more compact conformation with density similar to that of a folded protein. Neutron reflectivity shows that tau completely disrupts supported DMPG bilayers while leaving the neutral DPPC bilayer intact. Our results show that hTau40s strong interaction with anionic lipids induces tau structural compaction and membrane disruption, suggesting possible membrane-based mechanisms of tau aggregation and toxicity in neurodegenerative diseases