(Re)Imagining Relationality: Brad Isaacs and The Map of the Empire

The exhibition, The Map of the Empire (30 March – 6 May, 2016), featured photography, video, and installation works by Toronto-based artist, Brad Isaacs (Mohawk | mixed heritage). The majority of the artworks within the exhibition were produced from the Canadian Museum of Nature’s research and collections facility (Gatineau, Québec). The Canadian Museum of Nature (CMN), is the national natural history museum of (what is now called) Canada, with its galleries located in Ottawa, Ontario. The exhibition was the first to open at the Centre for Indigenous Research Creation at Queen’s University under the supervision of Dr. Dylan Robinson. Through the installment of The Map of the Empire, Isaacs effectively claimed space on campus grounds – within the geopolitical space of Katarokwi | Kingston – and pushed back against settler colonial imaginings of natural history. The Map of the Empire explored the capacity of Brad’s artistic practice in challenging the general belief under which natural history museums operate: that the experience of collecting/witnessing/interacting with a deceased and curated more-than-human animal will increase conservation awareness and facilitate human care towards nature. The exhibition also featured original poetry by Cecily Nicholson, author of Triage (2011) and From the Poplars (2014), as a response to Brad’s artwork. I locate the work of The Map of the Empire within the broader context of curatorship as a political practice engaging with conceptual and actualized forms of slow violence, both inside of and beyond the museum space. By unmapping the structures of slow, showcased and archived violence within the natural history museum, we can begin to radically transform and reimagine our connections with more-than-humans and encourage these relations to be reciprocal rather than hyper-curated or preserved.

Sequence and Structure Based Protein Folding Studies With Implications

As the expression of the genetic blueprint, proteins are at the heart of all biological systems. The ever increasing set of available protein structures has taught us that diversity is the hallmark of their architecture, a fundamental characteristic that enables them to perform the vast array of functionality upon which all of life depends. This diversity, however, is central to one of the most challenging problems in molecular biology: how does a folding polypeptide chain navigate its way through all of the myriad of possible conformations to find its own particular biologically active form? With few overarching structural principles to draw upon that can be applied to all protein architecture, the search for a solution to the protein folding problem has yet to produce an algorithm that can explain and duplicate this fundamental biological process. In this thesis, we take a two-pronged approach for investigating the protein folding process. Our initial statistical studies of the distributions of hydrophobic and hydrophilic residues within α-helices and β-sheets suggest (i) that hydrophobicity plays a critical role in helix and sheet formation; and (ii) that the nucleation of these motifs may result in largely unidirectional growth. Most tellingly, from an examination of the amino acids found in the smallest β-sheets, we do not find any evidence of a β-nucleating code in the primary protein sequence. Complementing these statistical analyses, we have analyzed the structural environments of several ever-widening aspects of protein topology. Our examination of the gaps between strands in the smallest β-sheets reveals a common organizational principle underlying β-formation involving strands separated by large sequential gaps: with very few exceptions, these large gaps fold into single, compact structural modules, bringing the β-strands that are otherwise far apart in the sequence close together in space. We conclude, therefore, that β-nucleation in the smallest sheets results from the co-location of two strands that are either local in sequence, or local in space following prior folding events. A second study of larger β-sheets both corroborates and extends these findings: virtually all large sequential gaps between pairs of β-strands organize themselves into an hierarchical arrangement, creating a bread-crumb model of go-and-come-back structural organization that ultimately juxtaposes two strands of a parental β-structure that are far apart in the sequence in close spatial proximity. In a final study, we have formalized this go-and-come-back notion into the concept of anti-parallel double-strandedness (DS), and measure this property across protein architecture in general. With over 90% of all residues in a large, non-redundant set of protein structures classified as DS, we conclude that DS is a unifying structural principle that underpins all globular proteins. We postulate, moreover, that this one simple principle, anti-parallel double-strandedness, unites protein structure, protein folding and protein evolution.