TITLE: Structural interrogation of small open reading frame (sORF) encoded proteins
ABSTRACT: Advances in genomics and proteomics have unearthed sequences of a startling number of novel proteins. Despite this, our knowledge of their three-dimensional structure and function relies on only a small fraction of the known protein universe. Small open reading frames (sORFs) encoding proteins less than 100 amino acids in length are an extreme example of this. With tens of thousands of newly discovered sORFs per year since the late 2000s, their gene products represent a kind of ‘dark matter’ of the proteome. Many sORF families encode sequences that do not resemble a known protein domain, limiting our ability to correlate their sequence to a known function. Given the widespread roles previously characterized small proteins play in bacterial cells, they hold great potential as future therapeutic targets. My current research is focussed on leveraging advances in protein structure prediction to discover sORF encoded proteins (SEP) with a compact tertiary structure and tease out the role they may be playing in cellular function.
