ASU Scholarship Showcase

This chapter is not a guide to embodied thinking, but rather a critical call to action. It highlights the deep history of embodied practice within the fields of dance and somatics, and outlines the value of embodied thinking within human-computer interaction (HCI) design and, more specifically, wearable technology (WT) design. What this chapter does not do is provide a guide or framework for embodied practice. As a practitioner and scholar grounded in the fields of dance and somatics, I argue that a guide to embodiment cannot be written in a book. To fully understand embodied thinking, one must act, move, and do. Terms such as embodiment and embodied thinking are often discussed and analyzed in writing; but if the purpose is to learn how to engage in embodied thinking, then the answers will not come from a text. The answers come from movement-based exploration, active trial-and-error, and improvisation practices crafted to cultivate physical attunement to one's own body. To this end, my "call to action" is for the reader to move beyond a text-based understanding of embodiment to active engagement in embodied methodologies. Only then, I argue, can one understand how to apply embodied thinking to a design process.

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma.

Results: This report describes the possibilities and limitations of performing such analyses based on the use of thionitrobenzoic acid and dimedone-based probes which are commonly employed to trap Cys-SOH. Results obtained by electrospray ionization-based mass spectrometric immunoassay reveal the optimal type of probe for such analyses as well as the reproducible relative quantification of Cys-SOH within albumin and transthyretin extracted from human plasma--the latter as a protein previously unknown to be modified by Cys-SOH.

Conclusions: The relative quantification of Cys-SOH within specific proteins in a complex biological setting can be accomplished, but several analytical precautions related to trapping, detecting, and quantifying Cys-SOH must be taken into account prior to pursuing its study in such matrices.