The interval and indoor playmaking

Although early modern acting companies were adept at using different kinds of venue, performing indoors imposed a significant change in practice. Since indoor theatres required artificial lighting to augment the natural light admitted via windows, candles were employed; but the technology was such that candles could not last untended throughout an entire performance. Performing indoors thus introduced a new component into stage practice: the interval. This article explores what extant evidence (such as it is) might tell us about the introduction of act breaks, how they may have worked, and the implications for actors, audiences and dramatists. Ben Jonson's scripting of the interval in two late plays, The Staple of News and The Magnetic Lady, is examined for what it may suggest about actual practice, and the ways in which the interval may have been considered integral to composition and performance is explored through a reading of Middleton and Rowley's The Changeling. The interval offered playwrights a form of structural punctuation, drawing attention to how acts ended and began; actors could use the space to bring on props for use in the next act; spectators might use the pause between acts to reflect on what had happened and, perhaps, anticipate what was to come; and stage-sitters, the evidence indicates, often took advantage of the hiatus in the play to assert their presence in the space to which all eyes naturally were drawn.

Insights into the molecular architecture of a peptide nanotube using FTIR and solid-state NMR spectroscopic measurements on an aligned sample

The self-assembly of proteins and peptides into b-sheet-rich amyloid fibers is a process that has gained notoriety because of its association with human diseases and disorders. Spontaneous self-assembly of peptides into nonfibrillar supramolecular structures can also provide a versatile and convenient mechanism for the bottom-up design of biocompatible materials with functional properties favoring a wide range of practical applications.[1] One subset of these fascinating and potentially useful nanoscale constructions are the peptide nanotubes, elongated cylindrical structures with a hollow center bounded by a thin wall of peptide molecules.[2] A formidable challenge in optimizing and harnessing the properties of nanotube assemblies is to gain atomistic insight into their architecture, and to elucidate precisely how the tubular morphology is constructed from the peptide building blocks. Some of these fine details have been elucidated recently with the use of magic-angle-spinning (MAS) solidstate NMR (SSNMR) spectroscopy.[3] MAS SSNMR measurements of chemical shifts and through-space interatomic distances provide constraints on peptide conformation (e.g., b-strands and turns) and quaternary packing. We describe here a new application of a straightforward SSNMR technique which, when combined with FTIR spectroscopy, reports quantitatively on the orientation of the peptide molecules within the nanotube structure, thereby providing an additional structural constraint not accessible to MAS SSNMR.