Getting Out From Under: Transcending Genre and Trauma

Nick and London haven’t seen each other in years, since college graduation, until London arrives at Nick’s bar one night, clearly in trouble. On a whim and with a surge of sympathy, Nick invites London to stay the night. This one night turns into many as the two have to maneuver living with the other, one struggling with mystery, the other with trust. Their walls slowly begin to come down and they fall in love. But London still has secrets that keep her closed off. It takes a lot of strength for her to reveal these secrets and get past what they mean. This project seeks to study how trauma can affect an individual and those around them. It is the story of London overcoming trauma in order to build relationships that have trust and transparency in them; to build relationships that allow her to fully be herself. The genre of chick lit plays a role in some of the conventions in the story, most notably with the romance that forms. The romance is actually a mode of healing for London which pushes back against the large feminist debate that romance plots are a patriarchal structure that don’t allow for autonomy. Getting Out From Under allows romance and autonomy and healing to coexist as well as thrive

Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation*

We investigated the ability of type I collagen telopeptides to bind neighboring collagen molecules, which is thought to be the initial event in fibrillogenesis. Limited hydrolysis by actinidain protease produced monomeric collagen, which consisted almost entirely of α1 and α2 chains. As seen with ultrahigh resolution scanning electron microscopy, actinidain-hydrolyzed collagen exhibited unique self-assembly, as if at an intermediate stage, and formed a novel suprastructure characterized by poor fibrillogenesis. Then, the N- and C-terminal sequences of chicken type I collagen hydrolyzed by actinidain or pepsin were determined by Edman degradation and de novo sequence analysis with matrix-assisted laser desorption ionization-tandem time-of-flight mass spectrometry, respectively. In the C-telopeptide region of the α1 chain, pepsin cleaved between Asp1035 and Phe1036, and actinidain between Gly1032 and Gly1033. Thus, the actinidain-hydrolyzed α1 chain is shorter at the C terminus by three residues, Gly1033, Phe1034, and Asp1035. In the α2 chain, both proteases cleaved between Glu1030 and Val1031. We demonstrated that a synthetic nonapeptide mimicking the α1 C-terminal sequence including GFD weakly inhibited the self-assembly of pepsin-hydrolyzed collagen, whereas it remarkably accelerated that of actinidain-hydrolyzed collagen. We conclude that the specific GFD sequence of the C-telopeptide of the α1 chain plays a crucial role in stipulating collagen suprastructure and in subsequent fibril formation