Raul Araya Secchi
In 2009 I enrolled into the Biotechnology PhD program of Universidad Andres Bello in Santiago (Chile) under the supervision of Dr. Tomas Perez-Acle and my research topic was the dynamics of water molecules inside the Connexin 26 (Cx26) hemichannel using molecular dynamics simulations. This work resulted in a thesis that got me a suma cum laude PhD degree. My thesis work resulted in three publications (Jara et al. Mol. Biol. Cell. 2012; Araya-Secchi et al. Biophys. J. 2014; Escalona et al. Biophys. J. 2016)
In December 2013 I moved to Columbus Ohio (USA) to start a postdoctoral position at The Ohio State University (OSU) under the supervision of Dr. Marcos Sotomayor. There I accomplished a long-sought dream: to learn protein X-ray crystallography. During this time, I worked in a project devoted to elucidating the structure and mechanical properties of proteins that form the inner-ear tip links, essential for hearing in mammals. My work resulted in the characterization of unique structural features of protocadherin15 that may play a key role in sound mechanotransduction. In this period, I participated in three high impact publications (Araya-Secchi et al. Nat. Commun. 2016; De-la-Torre et al. Biophys. J. 2018 and Choudary et al. PNAS. 2020) and one review (Jaiganesh et al. CSH Perspect. Biol. 2018).
In 2016 I moved to Copenhagen Denmark to start a second postdoctoral stay at University of Copenhagen under the supervision of Dr. Lise Arleth. Here I participated in an integrative structural biology project focused on the effect of membrane composition on the structure, dynamics, and function of membrane proteins. My work involved the integration of computer simulations with experimental data obtained by SAXS, SANS, NMR and Neutron Reflectometry (NR) of proteins samples embedded on lipid nano-discs or deposited on lipid covered surfaces. One of the biggest highlights of this work was the generation of the first structural model of GHR, a protein that contains a large, disordered region which makes it unamenable to typical structural biology approaches (Kassem, Araya-Secchi et. al. Science Advances. 2021).