Sofia N Barreira

The question of how proteins fold based on their amino acid sequences has been a long-standing challenge in the field of structural biology and, by extension, to the study of key biological questions in fields such as developmental and evolutionary biology. Historically, tertiary protein structures have been experimentally determined using labor-intensive techniques such as x-ray crystallography, nuclear magnetic resonance (NMR), and cryo-electron microscopy (CryoEM) [1].

Dynamics and distribution of 6mA during embryogenesis To quantitatively assess 6mA levels in Hydractinia, we extracted genomic DNA from adult specimens and from different embryonic stages. The samples were then enzymatically digested and purified. Synthetic oligonucleotides containing 6mA were similarly treated and used as external standards for ultra-high-performance liquid chromatography coupled with triple quadrupole tandem mass spectrometry (UHPLC-QQQ) (Fig 1A; pipeline on the left side).