Happy New Year everybody! Usually at this time of year I post about the O'Reilly Science Art holiday party of two, but the hubs and I couldn't secure a sitter this year. Instead, I am eager to announce a new series for this website. While I love doing The Short Answer and would be thrilled if anyone commissioned me to do one for their work, I had a feeling that after two years here it had run its course. So lately, I've been cooking up a new series that uses a more fine art-inspired brand of illustration to celebrate everyday discoveries in chemistry and biology. They won't be the stories you see in the New York Times or on Nova, but the indispensable yet unsung advances upon which those larger discoveries are built. So I give you, The Art of Basic Science.

The inaugural piece was inspired by a new tool that helps to show us what de-ubiquitylating enzymes are doing (see reference to paper below image). For a long time we thought of ubiquitylation as a simple tag for proteins on the way to the cellular landfill, but we are beginning to understand the dynamic and modular nature of this post-translational modification and its importance in a number of disorders. The artwork, loosely inspired by the likes of Klee and Kandinsky, is meant to illustrate the beauty of ubiquitin itself, its propensity for forming chains which are typically represented as a series of circles, and to invite you to imagine these circles being removed and replaced in a dynamic fashion.

Selenocysteine as a Latent Bioorthogonal Electrophilic Probe for Deubiquitylating Enzymes

Samuel D. Whedon, Nagula Markandeya, Ambar S. J. B. Rana, Nicholas A. Senger, Caroline E. Weller‡, Frantisek Tureček, Eric R. Strieter, and Champak Chatterjee

J. Am. Chem. Soc., 2016, 138 (42), pp 13774–13777