Visible Body Modification (VBM): Operationalizing Grooming Standards

The purpose of this study was to build on a previous one that focused on the effect of visible body modification (WM) on employment. In this study, samples from actual employee manuals used in the hospitality industry were collected and analyzed, specifically looking at policies regarding visible tattoos and body piercings. Examples from those employee manuals are presented, along with suggestions for operators looking to change or clarify their grooming standards.

Pressure induced structural changes and gas diffusion pathways in monomeric fluorescent proteins

Fluorescent proteins (FPs) are extremely valuable biochemical markers which have found a wide range of applications in cellular and molecular biology research. The monomeric variants of red fluorescent proteins (RFPs), known as mFruits, have been especially valuable for in vivo applications in mammalian cell imaging. Fluorescent proteins consist of a chromophore caged in the beta-barrel protein scaffold. The photophysical properties of an FP is determined by its chromophore structure and its interactions with the protein barrel. Application of hydrostatic pressure on FPs results in the modification of the chromophore environment which allows a systematic study of the role of the protein-chromophore interactions on photophysical properties of FPs. Using Molecular Dynamics (MD) computer simulations, I investigated the pressure induced structural changes in the monomeric variants mCherry, mStrawberry, and Citrine. The results explain the molecular basis for experimentally observed pressure responses among FP variants. It is found that the barrel flexibility, hydrogen bonding interactions and chromophore planarity of the FPs can be correlated to their contrasting photophysical properties at vaious pressures. I also investigated the oxygen diffusion pathways in mOrange and mOrange2 which exhibit marked differences in oxygen sensitivities as well as photostability. Such computational identifications of structural changes and oxygen diffusion pathways are important in guiding mutagenesis efforts to design fluorescent proteins with improved photophysical properties.

The Effects of Attention Bias Modification Training on Cognitive Biases Perceived Threats in Children with Anxiety

It has been found in research that children and adults with anxiety have a bias toward interpreting ambiguous situations as threatening. This bias is thought to consequently maintain many symptoms of anxiety. An emergent computer treatment system called Attention Bias Modification Training (ABMT) has been used to try to reduce this bias. It is essential to understand whether this bias can be reduced with ABMT because of its feasibility and cost effective nature of treatment. In the current study, interpretation bias is measured using the Children's Opinions of Everyday Life Events (COELE). The ABMT treatment is given to children once a week for an hour and their answers to the COELE are recorded before and after treatment. The recorded procedures are transcribed by undergraduate students working at the Child Anxiety and Phobia lab, and then scored. Each of the situations of the COELE are rated 0 being neutral or 1 threatening interpretation of the situation. The hypothesis is that ABMT will reduce the negative interpretation bias in children over the course of 4 weeks of treatment. The study is still in the collection and transcription of data phase, and will expect to have analytical conclusions in the start of spring 2015.

Pressure Induced Structural Changes and Gas Diffusion Pathways in Monomeric Fluorescent Proteins

Fluorescent proteins (FPs) are extremely valuable biochemical markers which have found a wide range of applications in cellular and molecular biology research. The monomeric variants of red fluorescent proteins (RFPs), known as mFruits, have been especially valuable for in vivo applications in mammalian cell imaging. Fluorescent proteins consist of a chromophore caged in the beta-barrel protein scaffold. The photophysical properties of an FP is determined by its chromophore structure and its interactions with the protein barrel. Application of hydrostatic pressure on FPs results in the modification of the chromophore environment which allows a systematic study of the role of the protein-chromophore interactions on photophysical properties of FPs. Using Molecular Dynamics (MD) computer simulations, I investigated the pressure induced structural changes in the monomeric variants mCherry, mStrawberry, and Citrine. The results explain the molecular basis for experimentally observed pressure responses among FP variants. It is found that the barrel flexibility, hydrogen bonding interactions and chromophore planarity of the FPs can be correlated to their contrasting photophysical properties at vaious pressures. I also investigated the oxygen diffusion pathways in mOrange and mOrange2 which exhibit marked differences in oxygen sensitivities as well as photostability. Such computational identifications of structural changes and oxygen diffusion pathways are important in guiding mutagenesis efforts to design fluorescent proteins with improved photophysical properties.