Fibronectin is an extracellular matrix protein involved in cell adhesion, proliferation and differentiation. In plasma, fibronectin exists as a soluble dimer, but cells mediate a process by which soluble fibronectin is converted to insoluble fibrils. This process can be mimicked, in vitro, by adding anastellin to fibronectin. Anastellin is a truncated form of the first type III domain of fibronectin (1FN3). The third type III domain (3FN3) is one of the binding sites for anastellin. Our research focuses on using nuclear magnetic resonance (NMR) spectroscopy to study the interaction between anastellin and fibronectin. However, thus far we have been unable to investigate the anastellin:3FN3 protein complex by traditional NMR spectroscopy, presumably due to conformational fluctuations. By participating in the East Asia and Pacific Summer Institutes (EAPSI) program, I was able to travel to Kinokawa, Japan to study protein dynamics using high-pressure NMR spectroscopy, which we do not have access to at my home institution. At the High Pressure Protein Research center, under the guidance of Professor Kazuyuki Akasaka, I investigated the effects of increased pressure on anastellin, 3FN3, and the anastellin:3FN3 complex. Analysis of the data collected this summer, and further experimentation, will allow us to better understand the stability and dynamics of the individual proteins and the complex. The EAPSI program also proved to be more than just an academic experience. While in Japan, I participated in several cultural programs and events allowing me to learn more about the Japanese culture and language. Some of the most gratifying experiences were helping others to learn English and being able to reconnect with my Japanese relatives. I am very grateful to have participated in the EAPSI program and I look forward to continuing to work with out new collaborators in Japan.